Evolutionary markers in the (β/α)8-barrel fold

[1]  Tsuyoshi Inoue,et al.  Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites. , 2003, Structure.

[2]  B. Stoddard,et al.  The 1.14 A crystal structure of yeast cytosine deaminase: evolution of nucleotide salvage enzymes and implications for genetic chemotherapy. , 2003, Structure.

[3]  T. Yeates,et al.  The crystal structure of the first enzyme in the pantothenate biosynthetic pathway, ketopantoate hydroxymethyltransferase, from M tuberculosis. , 2003, Structure.

[4]  D. Svergun,et al.  The active conformation of glutamate synthase and its binding to ferredoxin. , 2003, Journal of molecular biology.

[5]  Patricia C. Babbitt,et al.  Evolutionary Potential of (β/α)8-Barrels: Functional Promiscuity Produced by Single Substitutions in the Enolase Superfamily† , 2003 .

[6]  M. J. Jedrzejas,et al.  Identification and analysis of catalytic TIM barrel domains in seven further glycoside hydrolase families , 2003, FEBS letters.

[7]  P. Bork,et al.  Metabolites: a helping hand for pathway evolution? , 2003, Trends in biochemical sciences.

[8]  I. Wilson,et al.  Directed evolution of N-acetylneuraminic acid aldolase to catalyze enantiomeric aldol reactions. , 2003, Bioorganic & medicinal chemistry.

[9]  John Alan Gerlt,et al.  Evolution of function in (β/α)8-barrel enzymes , 2003 .

[10]  O. Mayans,et al.  Differential Regulation of a Hyperthermophilic α-Amylase with a Novel (Ca,Zn) Two-metal Center by Zinc* , 2003, The Journal of Biological Chemistry.

[11]  D. Hodgson,et al.  Occurrence of a putative ancient‐like isomerase involved in histidine and tryptophan biosynthesis , 2003, EMBO reports.

[12]  Thomas R. Schneider,et al.  Evolution of feedback-inhibited β/α barrel isoenzymes by gene duplication and a single mutation , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[13]  Masaru Goto,et al.  Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: open-closed conformational change and ammonia tunneling. , 2002, Journal of biochemistry.

[14]  M. Hennig,et al.  Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates. , 2002, Biochemistry.

[15]  J. C. Evans,et al.  Betaine-homocysteine methyltransferase: zinc in a distorted barrel. , 2002, Structure.

[16]  C. Orengo,et al.  One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. , 2002, Journal of molecular biology.

[17]  D. Schomburg,et al.  Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity. , 2002, Biochemistry.

[18]  Janet M Thornton,et al.  Pathway evolution, structurally speaking. , 2002, Current opinion in structural biology.

[19]  P. Babbitt,et al.  Homologous (β/α)8-Barrel enzymes that catalyze unrelated reactions: Orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase , 2002 .

[20]  Matthias Wilmanns,et al.  Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex. , 2002, Structure.

[21]  Sridar V. Chittur,et al.  Crystal Structure of Imidazole Glycerol Phosphate Synthase: A Tunnel through a (β/α)8 Barrel Joins Two Active Sites , 2001 .

[22]  H. Brinkmann,et al.  Archaeal Fructose-1,6-bisphosphate Aldolases Constitute a New Family of Archaeal Type Class I Aldolase* , 2001, The Journal of Biological Chemistry.

[23]  M. Wilmanns,et al.  Stability, catalytic versatility and evolution of the (βα ) 8 -barrel fold , 2001 .

[24]  V. Davisson,et al.  Subunit Interactions and Glutamine Utilization byEscherichia coli Imidazole Glycerol Phosphate Synthase , 2001, Journal of bacteriology.

[25]  R. Stevens,et al.  Combining structural genomics and enzymology: completing the picture in metabolic pathways and enzyme active sites. , 2000, Current opinion in structural biology.

[26]  P. Bork,et al.  Homology among (betaalpha)(8) barrels: implications for the evolution of metabolic pathways. , 2000, Journal of molecular biology.

[27]  M Wilmanns,et al.  Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion. , 2000, Science.

[28]  M Wilmanns,et al.  Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[29]  O. Herzberg,et al.  Helix swapping between two α/β barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg2+–oxalate , 1999 .

[30]  N. Jullian,et al.  Structure of the human glycogen‐associated protein phosphatase 1 regulatory subunit hGM: Homology modeling revealed an (α/β)8‐barrel‐like fold in the multidomain protein , 1999, Protein science : a publication of the Protein Society.

[31]  P C Babbitt,et al.  Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[32]  B Henrissat,et al.  Structural and sequence-based classification of glycoside hydrolases. , 1997, Current opinion in structural biology.

[33]  M. Hansson,et al.  Structure prediction and fold recognition for the ferrochelatase family of proteins , 1997, Proteins.

[34]  Georg A. Sprenger,et al.  Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the α/β barrel within the class I aldolase family , 1996 .

[35]  Š. Janeček.  Invariant glycines and prolines flanking in loops the strand β2 of various (α/β)8‐barrel enzymes: A hidden homology? , 1996, Protein science : a publication of the Protein Society.

[36]  P. Lio’,et al.  Histidine biosynthetic pathway and genes: structure, regulation, and evolution. , 1996, Microbiological reviews.

[37]  H. Jespersen,et al.  A circularly permuted α‐amylase‐type α/β‐barrel structure in glucan‐synthesizing glucosyltransferases , 1996 .

[38]  D Eisenberg,et al.  Inverse protein folding by the residue pair preference profile method: estimating the correctness of alignments of structurally compatible sequences. , 1995, Protein engineering.

[39]  P C Babbitt,et al.  A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids , 1995, Science.

[40]  M J Sternberg,et al.  Evaluation of the sequence template method for protein structure prediction. Discrimination of the (beta/alpha)8-barrel fold. , 1992, Journal of molecular biology.

[41]  M Wilmanns,et al.  Structural conservation in parallel beta/alpha-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis. , 1991, Biochemistry.

[42]  Gregory A. Petsko,et al.  The evolution of a/ barrel enzymes , 1990 .

[43]  K. Luger,et al.  Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo. , 1989, Science.

[44]  E. Padlan,et al.  Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. , 1988, The Journal of biological chemistry.

[45]  S J Wodak,et al.  Structural principles of parallel beta-barrels in proteins. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[46]  G N Cohen,et al.  Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[47]  Birte Höcker,et al.  Dissection of a (βα)8-barrel enzyme into two folded halves , 2001, Nature Structural Biology.

[48]  E. W. Miles.  Tryptophan synthase: a multienzyme complex with an intramolecular tunnel. , 2001, Chemical record.