Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima.
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M. Hennig | R. Thoma | R. Sterner | K. Kirschner | R Sterner | K Kirschner | R Thoma | M Hennig
[1] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[2] J. Navaza,et al. AMoRe: an automated package for molecular replacement , 1994 .
[3] J. Sambrook,et al. Molecular Cloning: A Laboratory Manual , 2001 .
[4] F. Studier,et al. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. , 1986, Journal of molecular biology.
[5] R Nussinov,et al. Hydrophobic folding units at protein‐protein interfaces: Implications to protein folding and to protein‐protein association , 1997, Protein science : a publication of the Protein Society.
[6] K. Kirschner,et al. The importance of surface loops for stabilizing an eightfold βα barrel protein , 1992 .
[7] N. Glansdorff,et al. The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[8] G. Taylor,et al. The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum. , 1994, Structure.
[9] N. Thanki,et al. Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies , 1996, Protein science : a publication of the Protein Society.
[10] K. Luger,et al. Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo. , 1989, Science.
[11] M Wilmanns,et al. Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution. , 1992, Journal of molecular biology.
[12] M. Page,et al. Structure and function of the dihydropteroate synthase from Staphylococcus aureus. , 1997, Journal of molecular biology.
[13] I. Crawford,et al. Enzymes of the Tryptophan Pathway in Three Bacillus Species , 1973, Journal of bacteriology.
[14] D. Hilvert,et al. Redesigning enzyme topology by directed evolution. , 1998, Science.
[15] R Abagyan,et al. Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8. , 1995, Structure.
[16] C. Matthews,et al. Construction and characterization of monomeric tryptophan repressor: a model for an early intermediate in the folding of a dimeric protein. , 1997, Biochemistry.
[17] D Eisenberg,et al. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. , 1997, Advances in protein chemistry.
[18] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[19] A. Miele,et al. Free energy of burying hydrophobic residues in the interface between protein subunits. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[20] R. Sterner,et al. (Beta alpha)8‐barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima. , 1995, The EMBO journal.
[21] W. Doolittle,et al. Genes for tryptophan biosynthesis in the halophilic archaebacterium Haloferax volcanii: the trpDFEG cluster , 1992, Journal of bacteriology.
[22] T. Traut. Dissociation of enzyme oligomers: a mechanism for allosteric regulation. , 1994, Critical reviews in biochemistry and molecular biology.
[23] W G Hol,et al. Three hTIM mutants that provide new insights on why TIM is a dimer. , 1996, Journal of molecular biology.
[24] A. Fersht,et al. Reversible dissociation of dimeric tyrosyl-tRNA synthetase by mutagenesis at the subunit interface. , 1985, Biochemistry.
[25] Disruption of Escherichia coli transaldolase into catalytically active monomers: evidence against half‐of‐the‐sites mechanism , 1998, FEBS letters.
[26] Z. Otwinowski,et al. [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[27] J. Martial,et al. Crystal structure of recombinant triosephosphate isomerase from bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three‐dimensional structures points to the importance of hydrophobic interactions , 1995, Protein science : a publication of the Protein Society.
[28] N. Thanki,et al. A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability. , 1997, Biochemistry.
[29] 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.
[30] G. Petsko,et al. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data , 1975, Nature.
[31] R. Nussinov,et al. Mechanism and evolution of protein dimerization , 1998, Protein science : a publication of the Protein Society.
[32] K. Kirschner,et al. Indoleglycerol phosphate synthase-phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains. , 1995, Biochemistry.
[33] G. Sarkar,et al. The "megaprimer" method of site-directed mutagenesis. , 1990, BioTechniques.
[34] G. Böhm,et al. The stability of proteins in extreme environments. , 1998, Current opinion in structural biology.
[35] R Abagyan,et al. The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: the correct modelling of an eight-residue loop. , 1993, Structure.
[36] K. Aune,et al. Analyses of sedimentation equilibrium data. , 1974, Analytical biochemistry.
[37] R. Hensel,et al. Dimeric 3‐Phosphoglycerate Kinases from Hyperthermophilic Archaea , 1995 .
[38] G. Braus,et al. The role of the TRP1 gene in yeast tryptophan biosynthesis. , 1988, The Journal of biological chemistry.
[39] R. Jaenicke,et al. Folding and association of oligomeric and multimeric proteins. , 2000, Advances in protein chemistry.
[40] K. Kirschner,et al. Phosphoribosyl anthranilate isomerase catalyzes a reversible amadori reaction. , 1995, Biochemistry.
[41] R. Jaenicke,et al. Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima. , 1999, Biochemistry.
[42] C. Pace,et al. How to measure and predict the molar absorption coefficient of a protein , 1995, Protein science : a publication of the Protein Society.
[43] R Abagyan,et al. Design, creation, and characterization of a stable, monomeric triosephosphate isomerase. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[44] M. Hennig,et al. Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability. , 1997, Biochemistry.
[45] R. Wells,et al. Expansion and Deletion of Triplet Repeat Sequences inEscherichia coli Occur on the Leading Strand of DNA Replication* , 1999, The Journal of Biological Chemistry.
[46] S. Ferreira,et al. Kinetics and energetics of subunit dissociation/unfolding of TIM: the importance of oligomerization for conformational persistence and chemical stability of proteins. , 1998, Biochemistry.
[47] A. Lustig,et al. Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer , 1996, Protein science : a publication of the Protein Society.