1ccj
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CONFORMER SELECTION BY LIGAND BINDING OBSERVED WITH PROTEIN CRYSTALLOGRAPHY
OverviewOverview
A large-scale movement between "closed" and "open" conformations of a, protein loop was observed directly with protein crystallography by, trapping individual conformers through binding of an exogenous ligand and, characterization with solution kinetics. The buried indole ring of Trp191, in cytochrome c peroxidase (CCP) was displaced by exogenous ligands, causing a conformational change of loop Pro190-Asn195 and exposing Trp191, to the protein surface. Kinetic measurements are consistent with a, two-step binding mechanism in which the rate-limiting step is a transition, of the protein to the open state, which then binds the ligand. This, large-scale conformational change of a functionally important region of, CCP is independent of ligand and indicates that about 4% of the wild-type, protein is in the open form in solution at any given time.
About this StructureAbout this Structure
1CCJ is a Single protein structure of sequence from Saccharomyces cerevisiae with HEM as ligand. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Protein conformer selection by ligand binding observed with crystallography., Cao Y, Musah RA, Wilcox SK, Goodin DB, McRee DE, Protein Sci. 1998 Jan;7(1):72-8. PMID:9514261
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