1ccj: Difference between revisions

Revision as of 13:04, 21 February 2008

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 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

Page seeded by OCA on Thu Feb 21 12:04:40 2008

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OCA

@@ Line 4: / Line 4: @@
 ==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, protein is in the open form in solution at any given time.
+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 Structure==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Cao, Y.]]
-[[Category: Goodin, D.B.]]
+[[Category: Goodin, D B.]]
-[[Category: Mcree, D.E.]]
+[[Category: Mcree, D E.]]
-[[Category: Musah, R.A.]]
+[[Category: Musah, R A.]]
-[[Category: Wilcox, S.K.]]
+[[Category: Wilcox, S K.]]
 [[Category: HEM]]
 [[Category: oxidoreductase]]
 [[Category: peroxidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:34:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:40 2008''