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Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights.

Acta Crystallogr D Biol Crystallogr 58 2009-17 (2002)
Cited: 45 times
EuropePMC logo PMID: 12454458

Abstract

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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  1. Evolutionarily conserved amino acids that control TCR-MHC interaction. Marrack P, Scott-Browne JP, Dai S, Gapin L, Kappler JW. Annu Rev Immunol 26 171-203 (2008)

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