DOI Link]
Yousef MS, Fabiola F, Gattis JL, Somasundaram T, Chapman MS.
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL
32306-4380, USA.
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.
PMID: 12454458 [PubMed - indexed for MEDLINE]
This publication is one of the several that describes a structure solved either at the Kasha Laboratory, Institute of Molecular Biophysics
or in collaboration with the Institute Faculty. The data used for this structure determination came in full or part from the
Macromolecular X-Ray Crystallography Facility.
