1m15

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{{STRUCTURE_1m15| PDB=1m15 | SCENE= }}
{{STRUCTURE_1m15| PDB=1m15 | SCENE= }}
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'''TRANSITION STATE STRUCTURE OF ARGININE KINASE'''
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===TRANSITION STATE STRUCTURE OF ARGININE KINASE===
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==Overview==
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The three-dimensional crystal structure of an arginine kinase transition-state analogue complex has been refined at 1.2 A resolution, with an overall R factor of 12.3%. The current model provides a unique opportunity to analyze the structure of a bimolecular (phosphagen kinase) enzyme in its transition state. This atomic resolution structure confirms in-line transfer of the phosphoryl group and the catalytic importance of the precise alignment of the substrates. The structure is consistent with a concerted proton transfer that has been proposed for an unrelated kinase. Refinement of anisotropic temperature factors and translation-libration-screw (TLS) analyses led to the identification of four rigid groups and their prevalent modes of motion in the transition state. The relative magnitudes of the mobility of rigid groups are consistent with their proposed roles in catalysis.
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(as it appears on PubMed at http://www.pubmed.gov), where 12454458 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12454458}}
==About this Structure==
==About this Structure==
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[[Category: Phosphagen kinase]]
[[Category: Phosphagen kinase]]
[[Category: Transition state analog]]
[[Category: Transition state analog]]
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Revision as of 19:59, 2 July 2008

Image:1m15.png

Template:STRUCTURE 1m15

TRANSITION STATE STRUCTURE OF ARGININE KINASE

Template:ABSTRACT PUBMED 12454458

About this Structure

1M15 is a Single protein structure of sequence from Limulus polyphemus. Full crystallographic information is available from OCA.

Reference

Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights., Yousef MS, Fabiola F, Gattis JL, Somasundaram T, Chapman MS, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2009-17. Epub 2002, Nov 23. PMID:12454458

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