1M15

Transition state structure of arginine kinase

Summary for 1M15

• Entry DOI: 10.2210/pdb1m15/pdb
• Descriptor: arginine kinase, NITRATE ION, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: arginine kinase, creatine kinase, phosphagen kinase, transition state analog, adenosine triphosphate, transferase
• Biological source: Limulus polyphemus (Atlantic horseshoe crab)
• Total number of polymer chains: 1
• Total formula weight: 41000.48

Authors

Yousef, M.S.,Fabiola, F.,Gattis, J.L.,Somasundaram, T.,Chapman, M.S. (deposition date: 2002-06-17, release date: 2002-12-04, Last modification date: 2024-02-14)

Primary citation

Yousef, M.S.,Fabiola, F.,Gattis, J.L.,Somasundaram, T.,Chapman, M.S.
Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights.
Acta Crystallogr.,Sect.D, 58:2009-2017, 2002

PubMed 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.

PubMed: 12454458
DOI: 10.1107/S0907444902014683

Experimental method

X-RAY DIFFRACTION (1.2 Å)