1ccj
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(New page: 200px<br /> <applet load="1ccj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ccj, resolution 2.1Å" /> '''CONFORMER SELECTION ...)
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Revision as of 14:48, 29 October 2007
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CONFORMER SELECTION BY LIGAND BINDING OBSERVED WITH PROTEIN CRYSTALLOGRAPHY
Overview
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, ... [(full description)]
About this Structure
1CCJ is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM as [ligand]. Active as [[1]], with EC number [1.11.1.5]. Full crystallographic information is available from [OCA].
Reference
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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