1CCJ

CONFORMER SELECTION BY LIGAND BINDING OBSERVED WITH PROTEIN CRYSTALLOGRAPHY

Summary for 1CCJ

• Entry DOI: 10.2210/pdb1ccj/pdb
• Descriptor: CYTOCHROME C PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: oxidoreductase, peroxidase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Mitochondrion matrix: P00431
• Total number of polymer chains: 1
• Total formula weight: 34113.78

Authors

Cao, Y.,Musah, R.A.,Wilcox, S.K.,Goodin, D.B.,Mcree, D.E. (deposition date: 1997-01-22, release date: 1997-07-23, Last modification date: 2024-05-22)

Primary citation

Cao, Y.,Musah, R.A.,Wilcox, S.K.,Goodin, D.B.,McRee, D.E.
Protein conformer selection by ligand binding observed with crystallography.
Protein Sci., 7:72-78, 1998

PubMed Abstract: 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.

PubMed: 9514261

Experimental method

X-RAY DIFFRACTION (2.1 Å)