Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution
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Multiple protein structure alignmentCan sequence determine function?The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridgesStabilization of a (betaalpha)8-barrel protein by an engineered disulfide bridgeA monomeric TIM-barrel structure from Pyrococcus furiosus is optimized for extreme temperaturesCharacterization of the indole-3-glycerol phosphate synthase from Pseudomonas aeruginosa PAO1Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold.Solvent accessibility and purifying selection within proteins of Escherichia coli and Salmonella enterica.The ups and downs of protein topology; rapid comparison of protein structure.Structural similarity to link sequence space: new potential superfamilies and implications for structural genomics.Protein pockets: inventory, shape, and comparisonA study in molecular contingency: glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomerase.Betaalpha-hairpin clamps brace betaalphabeta modules and can make substantive contributions to the stability of TIM barrel proteins.The critical role of N- and C-terminal contact in protein stability and folding of a family 10 xylanase under extreme conditions.PoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimalityInter-Protein Sequence Co-Evolution Predicts Known Physical Interactions in Bacterial Ribosomes and the Trp OperonThree-dimensional profiles from residue-pair preferences: identification of sequences with beta/alpha-barrel foldMutational analysis of the active site of indoleglycerol phosphate synthase from Escherichia coli.Formation of the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase by a disorder-order transition from the unactivated to the activated form.Multifunctional tryptophan-synthesizing enzyme. The molecular weight of the Euglena gracilis protein is unexpectedly low.Functions of the gene products of Escherichia coli.Functional identification of the general acid and base in the dehydration step of indole-3-glycerol phosphate synthase catalysis.Evolutionally guided enzyme design.(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima.Crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon Thermococcus kodakaraensis.Modeling and docking the endothelin G-protein-coupled receptor.Parallel beta/alpha-barrels of alpha-amylase, cyclodextrin glycosyltransferase and oligo-1,6-glucosidase versus the barrel of beta-amylase: evolutionary distance is a reflection of unrelated sequences.Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer.Divergent evolution of a beta/alpha-barrel subclass: detection of numerous phosphate-binding sites by motif search.Invariant glycines and prolines flanking in loops the strand beta 2 of various (alpha/beta)8-barrel enzymes: a hidden homology?Adaptation of class-13 alpha-amylases to diverse living conditions.Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus.In vivo fragment complementation of a (beta/alpha)(8) barrel protein: generation of variability by recombination.A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.Functional classification of protein structures by local structure matching in graph representation.Roles for the two N-terminal (β/α) modules in the folding of a (β/α)₈-barrel protein as studied by fragmentation analysis.
P2860
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P2860
Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution
description
1992 nî lūn-bûn
@nan
1992 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Three-dimensional structure of ...... li refined at 2.0 A resolution
@ast
Three-dimensional structure of ...... li refined at 2.0 A resolution
@en
Three-dimensional structure of ...... li refined at 2.0 A resolution
@nl
type
label
Three-dimensional structure of ...... li refined at 2.0 A resolution
@ast
Three-dimensional structure of ...... li refined at 2.0 A resolution
@en
Three-dimensional structure of ...... li refined at 2.0 A resolution
@nl
prefLabel
Three-dimensional structure of ...... li refined at 2.0 A resolution
@ast
Three-dimensional structure of ...... li refined at 2.0 A resolution
@en
Three-dimensional structure of ...... li refined at 2.0 A resolution
@nl
P2093
P1476
Three-dimensional structure of ...... li refined at 2.0 A resolution
@en
P2093
J N Jansonius
J P Priestle
M Wilmanns
T Niermann
P304
P356
10.1016/0022-2836(92)90665-7
P407
P577
1992-01-20T00:00:00Z