A database of macromolecular motions.

We describe a database of macromolecular motions meant to be of general use to the structural community. The database, which is accessible on the World Wide Web with an entry point at http://bioinfo.mbb.yale.edu/MolMovDB , attempts to systematize all instances of protein and nucleic acid movement for which there is at least some structural information. At present it contains >120 motions, most of which are of proteins. Protein motions are further classified hierarchically into a limited number of categories, first on the basis of size (distinguishing between fragment, domain and subunit motions) and then on the basis of packing. Our packing classification divides motions into various categories (shear, hinge, other) depending on whether or not they involve sliding over a continuously maintained and tightly packed interface. In addition, the database provides some indication about the evidence behind each motion (i.e. the type of experimental information or whether the motion is inferred based on structural similarity) and attempts to describe many aspects of a motion in terms of a standardized nomenclature (e.g. the maximum rotation, the residue selection of a fixed core, etc.). Currently, we use a standard relational design to implement the database. However, the complexity and heterogeneity of the information kept in the database makes it an ideal application for an object-relational approach, and we are moving it in this direction. Specifically, in terms of storing complex information, the database contains plausible representations for motion pathways, derived from restrained 3D interpolation between known endpoint conformations. These pathways can be viewed in a variety of movie formats, and the database is associated with a server that can automatically generate these movies from submitted coordinates.

[1]  F. Young Biochemistry , 1955, The Indian Medical Gazette.

[2]  E. Antonini,et al.  HEMOGLOBIN AND MYOGLOBIN. , 1964, Advances in protein chemistry.

[3]  I. H. Segel,et al.  Glycogen phosphorylase of , 1969 .

[4]  Daniel E. Koshland,et al.  Protein Shape and Biological Control , 1973 .

[5]  F M Richards,et al.  Areas, volumes, packing and protein structure. , 1977, Annual review of biophysics and bioengineering.

[6]  T. Steitz,et al.  Glucose-induced conformational change in yeast hexokinase. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[7]  K. Waltersson,et al.  The crystal structure of Cs[VOF3] · 12H2O , 1979 .

[8]  T. Steitz,et al.  Space-filling models of kinase clefts and conformation changes. , 1979, Science.

[9]  Abraham Silberschatz,et al.  Database System Concepts , 1980 .

[10]  R. Huber,et al.  Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution. , 1984, Journal of molecular biology.

[11]  Hans Frauenfelder,et al.  Dynamics of Proteins , 1982 .

[12]  S. Harrison,et al.  Structure of tomato busy stunt virus IV. The virus particle at 2.9 A resolution. , 1983, Journal of molecular biology.

[13]  J. Janin,et al.  Structural domains in proteins and their role in the dynamics of protein function. , 1983, Progress in biophysics and molecular biology.

[14]  Arthur J. Olson,et al.  Structure of tomato bushy stunt virus IVThe virus particle at 29resolution , 1983 .

[15]  Cyrus Chothia,et al.  Transmission of conformational change in insulin , 1983, Nature.

[16]  A M Lesk,et al.  Mechanisms of domain closure in proteins. , 1984, Journal of molecular biology.

[17]  F. M. Richards,et al.  Calculation of molecular volumes and areas for structures of known geometry. , 1985, Methods in enzymology.

[18]  F. Cohen,et al.  A "helix-scissors" mechanism for the hinge-bending conformational change in phosphoglycerate kinase. , 2009, International journal of peptide and protein research.

[19]  Michael Stonebraker,et al.  The design of POSTGRES , 1986, SIGMOD '86.

[20]  W. Kent,et al.  Proceedings of the Thirteenth International Conference on Very Large Data Bases, Brighton, England, 1987 , 1987 .

[21]  J L Sussman,et al.  Refined crystal structure of dogfish M4 apo-lactate dehydrogenase. , 1989, Journal of molecular biology.

[22]  Michael Stonebraker,et al.  The POSTGRES Data Model , 1987, Research Foundations in Object-Oriented and Semantic Database Systems.

[23]  J. Ponder,et al.  Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. , 1987, Journal of molecular biology.

[24]  Z Otwinowski,et al.  Flexibility of the DNA‐binding domains of trp repressor , 1988, Proteins.

[25]  A. Cooper Dynamics of Proteins and Nucleic Acids , 1988 .

[26]  A. Lesk,et al.  Elbow motion in the immunoglobulins involves a molecular ball-and-socket joint , 1988, Nature.

[27]  K. Moffat Time-resolved macromolecular crystallography , 1996 .

[28]  M Karplus,et al.  Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. , 1990, Science.

[29]  Max F. Perutz,et al.  Mechanisms of Cooperativity and Allosteric Regulation in Proteins , 1990 .

[30]  Steven C. Almo,et al.  Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis , 1990, Nature.

[31]  F E Cohen,et al.  Novel method for the rapid evaluation of packing in protein structures. , 1990, Journal of molecular biology.

[32]  W. Mangel,et al.  Characterization of an extremely large, ligand-induced conformational change in plasminogen. , 1990, Science.

[33]  R. Stevens,et al.  Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution. , 1990, Biochemistry.

[34]  Edward N. Baker,et al.  Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins , 1990, Nature.

[35]  Raymond C. Stevens,et al.  Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution. , 1990 .

[36]  C. Chothia,et al.  Serpin tertiary structure transformation. , 1991, Journal of molecular biology.

[37]  M. Noble,et al.  The crystal structure of the “open” and the “closed” conformation of the flexible loop of trypanosomal triosephosphate isomerase , 1991, Proteins.

[38]  Philip R. Evans,et al.  Structural aspects of allostery , 1991 .

[39]  J. Knowles,et al.  Enzyme catalysis: not different, just better , 1991, Nature.

[40]  M Gerstein,et al.  Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase. , 1991, Journal of molecular biology.

[41]  D. Moras,et al.  Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp) , 1991, Science.

[42]  P. Kraulis A program to produce both detailed and schematic plots of protein structures , 1991 .

[43]  F A Quiocho,et al.  Comparison of the periplasmic receptors for L-arabinose, D-glucose/D-galactose, and D-ribose. Structural and Functional Similarity. , 1991, The Journal of biological chemistry.

[44]  J. Knowles,et al.  To build an enzyme.... , 1991, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[45]  S. Opella,et al.  NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein. , 1991, Science.

[46]  W. Kabsch,et al.  Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[47]  Axel T. Brunger,et al.  X-PLOR Version 3.1: A System for X-ray Crystallography and NMR , 1992 .

[48]  F A Quiocho,et al.  Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. , 1992, Science.

[49]  I. Kuntz Structure-Based Strategies for Drug Design and Discovery , 1992, Science.

[50]  J. Knowles,et al.  Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase. , 1992, Biochemistry.

[51]  C. Chothia One thousand families for the molecular biologist , 1992, Nature.

[52]  A. R. Srinivasan,et al.  The nucleic acid database. A comprehensive relational database of three-dimensional structures of nucleic acids. , 1992, Biophysical journal.

[53]  R. Stevens,et al.  A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamoylase. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[54]  A. Bairoch,et al.  The SWISS-PROT protein sequence data bank. , 1991, Nucleic acids research.

[55]  K Harlos,et al.  Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3‐phospho‐D‐glycerate , 1992, Proteins.

[56]  A M Lesk,et al.  Domain closure in mitochondrial aspartate aminotransferase. , 1992, Journal of molecular biology.

[57]  AC Tose Cell , 1993, Cell.

[58]  F M Richards,et al.  An analysis of packing in the protein folding problem , 1993, Quarterly Reviews of Biophysics.

[59]  M Gerstein,et al.  Domain closure in lactoferrin. Two hinges produce a see-saw motion between alternative close-packed interfaces. , 1993, Journal of molecular biology.

[60]  P. Sharp,et al.  Crystal structure of yeast TATA-binding protein and model for interaction with DNA. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[61]  Steven Hahn,et al.  Crystal structure of a yeast TBP/TATA-box complex , 1993, Nature.

[62]  D A Winkelmann,et al.  Three-dimensional structure of myosin subfragment-1: a molecular motor. , 1993, Science.

[63]  V. P. Chuprina,et al.  Structure of the complex of lac repressor headpiece and an 11 base-pair half-operator determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics. , 1994, Journal of Molecular Biology.

[64]  M. Gerstein,et al.  Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. , 1993, The EMBO journal.

[65]  J A McCammon,et al.  Gating of the active site of triose phosphate isomerase: Brownian dynamics simulations of flexible peptide loops in the enzyme. , 1993, Biophysical journal.

[66]  M Gerstein,et al.  Domain closure in adenylate kinase. Joints on either side of two helices close like neighboring fingers. , 1993, Journal of molecular biology.

[67]  C. Sander,et al.  The FSSP database of structurally aligned protein fold families. , 1994, Nucleic acids research.

[68]  J L Sussman,et al.  Open "back door" in a molecular dynamics simulation of acetylcholinesterase. , 1994, Science.

[69]  A. Lesk,et al.  Structural mechanisms for domain movements in proteins. , 1994, Biochemistry.

[70]  Gregory D. Schuler,et al.  WWW Entrez: A Hypertext Retrieval Tool for Molecular Biology. , 1994 .

[71]  David T. Jones,et al.  Protein superfamilles and domain superfolds , 1994, Nature.

[72]  M Gerstein,et al.  Volume changes on protein folding. , 1994, Structure.

[73]  J. Skehel,et al.  Structure of influenza haemagglutinin at the pH of membrane fusion , 1994, Nature.

[74]  K. Flaherty,et al.  Three-dimensional structure of a hammerhead ribozyme , 1994, Nature.

[75]  P. Argos,et al.  Cavities and packing at protein interfaces , 1994, Protein science : a publication of the Protein Society.

[76]  M. Gerstein,et al.  Average core structures and variability measures for protein families: application to the immunoglobulins. , 1995, Journal of molecular biology.

[77]  A G Murzin,et al.  SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.

[78]  R A Sayle,et al.  RASMOL: biomolecular graphics for all. , 1995, Trends in biochemical sciences.

[79]  A. Klug,et al.  The crystal structure of an AII-RNAhammerhead ribozyme: A proposed mechanism for RNA catalytic cleavage , 1995, Cell.

[80]  M J Rooman,et al.  Automatic analysis of protein conformational changes by multiple linkage clustering. , 1995, Journal of molecular biology.

[81]  A. Aggarwal,et al.  Structure of Bam HI endonuclease bound to DNA: partial folding and unfolding on DNA binding. , 1995, Science.

[82]  G. Schulz,et al.  Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. , 1995, Structure.

[83]  Richard M. Stallman,et al.  Gnu Emacs Manual , 1996 .

[84]  C Sander,et al.  Mapping the Protein Universe , 1996, Science.

[85]  C. Kundrot,et al.  Crystal Structure of a Group I Ribozyme Domain: Principles of RNA Packing , 1996, Science.

[86]  Eugene V. Koonin,et al.  [18] Protein sequence comparison at genome scale , 1996 .

[87]  D. Moras,et al.  Conformational flexibility of tRNA: structural changes in yeast tRNA(Asp) upon binding to aspartyl-tRNA synthetase. , 1996, Biochimie.

[88]  S H Bryant,et al.  A dynamic look at structures: WWW-Entrez and the Molecular Modeling Database. , 1996, Trends in biochemical sciences.

[89]  P Argos,et al.  A functional role for protein cavities in domain: domain motions. , 1996, Journal of molecular biology.

[90]  M Gerstein,et al.  Packing at the protein-water interface. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[91]  Amos Bairoch,et al.  The PROSITE database, its status in 1995 , 1996, Nucleic Acids Res..

[92]  H. Wolfson,et al.  A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique. , 1996, Journal of molecular biology.

[93]  G. Chang,et al.  Crystal Structure of the Lactose Operon Repressor and Its Complexes with DNA and Inducer , 1996, Science.

[94]  S. Mowbray,et al.  Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: the maltose-, glucose/galactose- and ribose-binding proteins. , 1996, Journal of molecular biology.

[95]  C. Schutt,et al.  The structure of an open state of beta-actin at 2.65 A resolution. , 1996, Journal of molecular biology.

[96]  E. Koonin,et al.  Protein sequence comparison at genome scale. , 1996, Methods in enzymology.

[97]  Tim J. P. Hubbard,et al.  SCOP: a structural classification of proteins database , 1998, Nucleic Acids Res..

[98]  Wilfried Schildkamp,et al.  Structure of a Protein Photocycle Intermediate by Millisecond Time-Resolved Crystallography , 1997, Science.

[99]  F E Cohen,et al.  A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform. , 1997, Journal of molecular biology.

[100]  M Gerstein,et al.  A structural census of genomes: comparing bacterial, eukaryotic, and archaeal genomes in terms of protein structure. , 1997, Journal of molecular biology.

[101]  Deborah Fass,et al.  Core Structure of gp41 from the HIV Envelope Glycoprotein , 1997, Cell.

[102]  Russ B. Altman,et al.  RIBOWEB: Linking Structural Computations to a Knowledge Base of Published Experimental Data , 1997, ISMB.

[103]  N Williams,et al.  How to Get Databases Talking the Same Language , 1997, Science.

[104]  F E Cohen,et al.  The prion folding problem. , 1997, Current opinion in structural biology.

[105]  Amos Bairoch,et al.  The PROSITE database, its status in 1997 , 1997, Nucleic Acids Res..

[106]  C. Chothia,et al.  Population statistics of protein structures: lessons from structural classifications. , 1997, Current opinion in structural biology.

[107]  P E Wright,et al.  Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[108]  M. Gerstein,et al.  LPFC: An internet library of protein family core structures , 1997, Protein science : a publication of the Protein Society.

[109]  M. Levitt,et al.  Protein folding: the endgame. , 1997, Annual review of biochemistry.

[110]  Russ B. Altman,et al.  Standardized Representations of the Literature: Combining Diverse Sources of Ribosomal Data , 1997, ISMB.

[111]  J L Sussman,et al.  Protein Data Bank archives of three-dimensional macromolecular structures. , 1997, Methods in enzymology.

[112]  M. Gerstein,et al.  Comparing genomes in terms of protein structure: surveys of a finite parts list. , 1998, FEMS microbiology reviews.