1m15
TRANSITION STATE STRUCTURE OF ARGININE KINASE
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OverviewOverview
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.
About this StructureAbout this Structure
1M15 is a Single protein structure of sequence from Limulus polyphemus with NO3, MG, ARG and ADP as ligands. Active as Transferase, with EC number 2.7.3.3. Full crystallographic information is available from OCA.
ReferenceReference
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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