2rh5

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{{Seed}}
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{{STRUCTURE_2rh5| PDB=2rh5 | SCENE= }}
{{STRUCTURE_2rh5| PDB=2rh5 | SCENE= }}
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'''Structure of Apo Adenylate Kinase from Aquifex Aeolicus'''
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===Structure of Apo Adenylate Kinase from Aquifex Aeolicus===
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==Overview==
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The mechanisms by which enzymes achieve extraordinary rate acceleration and specificity have long been of key interest in biochemistry. It is generally recognized that substrate binding coupled to conformational changes of the substrate-enzyme complex aligns the reactive groups in an optimal environment for efficient chemistry. Although chemical mechanisms have been elucidated for many enzymes, the question of how enzymes achieve the catalytically competent state has only recently become approachable by experiment and computation. Here we show crystallographic evidence for conformational substates along the trajectory towards the catalytically competent 'closed' state in the ligand-free form of the enzyme adenylate kinase. Molecular dynamics simulations indicate that these partially closed conformations are sampled in nanoseconds, whereas nuclear magnetic resonance and single-molecule fluorescence resonance energy transfer reveal rare sampling of a fully closed conformation occurring on the microsecond-to-millisecond timescale. Thus, the larger-scale motions in substrate-free adenylate kinase are not random, but preferentially follow the pathways that create the configuration capable of proficient chemistry. Such preferred directionality, encoded in the fold, may contribute to catalysis in many enzymes.
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(as it appears on PubMed at http://www.pubmed.gov), where 18026086 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18026086}}
==About this Structure==
==About this Structure==
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[[Category: Kinase]]
[[Category: Kinase]]
[[Category: Nucleotide-binding]]
[[Category: Nucleotide-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:54:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:12:38 2008''

Revision as of 20:12, 28 July 2008

Image:2rh5.png

Template:STRUCTURE 2rh5

Structure of Apo Adenylate Kinase from Aquifex Aeolicus

Template:ABSTRACT PUBMED 18026086

About this Structure

2RH5 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

Intrinsic motions along an enzymatic reaction trajectory., Henzler-Wildman KA, Thai V, Lei M, Ott M, Wolf-Watz M, Fenn T, Pozharski E, Wilson MA, Petsko GA, Karplus M, Hubner CG, Kern D, Nature. 2007 Dec 6;450(7171):838-44. Epub 2007 Nov 18. PMID:18026086

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