1M15: Transition State Structure Of Arginine Kinase

Citation:
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.
PDB ID: 1M15Download
MMDB ID: 21194
PDB Deposition Date: 2002/6/17
Updated in MMDB: 2002/12
Experimental Method:
x-ray diffraction
Resolution: 1.2  Å
Source Organism:
Similar Structures:
Biological Unit for 1M15: monomeric; determined by author and by software (PISA)
Molecular Components in 1M15
Label Count Molecule
Protein (1 molecule)
1
Arginine Kinase
Molecule annotation
Chemicals (5 molecules)
1
2
2
1
3
1
4
1
* Click molecule labels to explore molecular sequence information.

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