1bg0: Difference between revisions

Revision as of 19:04, 30 June 2008

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File:1bg0.png

Template:STRUCTURE 1bg0

TRANSITION STATE STRUCTURE OF ARGININE KINASETRANSITION STATE STRUCTURE OF ARGININE KINASE

Template:ABSTRACT PUBMED 9671698

About this StructureAbout this Structure

1BG0 is a Single protein structure of sequence from Limulus polyphemus. Full crystallographic information is available from OCA.

ReferenceReference

Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions., Zhou G, Somasundaram T, Blanc E, Parthasarathy G, Ellington WR, Chapman MS, Proc Natl Acad Sci U S A. 1998 Jul 21;95(15):8449-54. PMID:9671698

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OCA

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-'''TRANSITION STATE STRUCTURE OF ARGININE KINASE'''
+===TRANSITION STATE STRUCTURE OF ARGININE KINASE===
-==Overview==
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-Arginine kinase belongs to the family of enzymes, including creatine kinase, that catalyze the buffering of ATP in cells with fluctuating energy requirements and that has been a paradigm for classical enzymological studies. The 1.86-A resolution structure of its transition-state analog complex, reported here, reveals its active site and offers direct evidence for the importance of precise substrate alignment in the catalysis of bimolecular reactions, in contrast to the unimolecular reactions studied previously. In the transition-state analog complex studied here, a nitrate mimics the planar gamma-phosphoryl during associative in-line transfer between ATP and arginine. The active site is unperturbed, and the reactants are not constrained covalently as in a bisubstrate complex, so it is possible to measure how precisely they are pre-aligned by the enzyme. Alignment is exquisite. Entropic effects may contribute to catalysis, but the lone-pair orbitals are also aligned close enough to their optimal trajectories for orbital steering to be a factor during nucleophilic attack. The structure suggests that polarization, strain toward the transition state, and acid-base catalysis also contribute, but, in contrast to unimolecular enzyme reactions, their role appears to be secondary to substrate alignment in this bimolecular reaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_9671698}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Transferase]]
 [[Category: Transition state analog]]
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