(Q43024589)

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Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus.

scientific article published in May 1997

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3 November 2019

Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus (English)

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3 November 2019

Zaida Luthey-Schulten

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3 November 2019

Peter Guy Wolynes

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P G Wolynes

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3 November 2019

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P Haney

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3 November 2019

J Konisky

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3 November 2019

K K Koretke

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1 May 1997

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3 November 2019

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3 November 2019

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3 November 2019

117-130

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3 November 2019

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3 November 2019

Temperature adaptation of lactate dehydrogenase. Structural, functional and genetic aspects

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Engineering protein thermal stability. Sequence statistics point to residue substitutions in alpha-helices.

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Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus

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Heat stability of a tetrameric enzyme, D-glyceraldehyde-3-phosphate dehydrogenase

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Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

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Protein stability and molecular adaptation to extreme conditions

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Proteins under extreme physical conditions

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Structural and genetic analysis of protein stability

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The adenylate kinases from a mesophilic and three thermophilic methanogenic members of the Archaea

1 reference

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The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP

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The structure of uridylate kinase with its substrates, showing the transition state geometry.

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Substrate specificity and assembly of the catalytic center derived from two structures of ligated uridylate kinase

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Crystal structure of the complex of UMP/CMP kinase from Dictyostelium discoideum and the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-uridyl) pentaphosphate (UP5A) and Mg2+ at 2.2 A: implications for water-mediated specificity

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Identification, cloning, and expression of the gene for adenylate kinase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

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Adenylate kinase from Sulfolobus acidocaldarius: expression in Escherichia coli and characterization by Fourier transform infrared spectroscopy.

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Protein tertiary structure recognition using optimized Hamiltonians with local interactions

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The Protein Data Bank: a computer-based archival file for macromolecular structures

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Evaluation of comparative protein modeling by MODELLER

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Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment

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Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models

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The mechanisms of irreversible enzyme inactivation at 100C.

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Arginine residues as stabilizing elements in proteins

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Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli.

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Mechanism of adenylate kinase. Are the essential lysines essential?

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Mechanism of adenylate kinase. Structural and functional roles of the conserved arginine-97 and arginine-132.

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The glycine-rich loop of adenylate kinase forms a giant anion hole

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Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state

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Refined structure of porcine cytosolic adenylate kinase at 2.1 A resolution

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21 January 2018

Identifiers

10.1002/(SICI)1097-0134(199705)28:1<117::AID-PROT12>3.0.CO;2-M

1 reference

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3 November 2019

1 reference

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3 November 2019

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