1cpr
From Proteopedia
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ST. LOUIS CYTOCHROME C' FROM THE PURPLE PHOTOTROPIC BACTERIUM, RHODOBACTER CAPSULATUS
Overview
Rhodobacter capsulatus strain St Louis cytochrome c' (RCCP-SL) has been, crystallized and the structure solved by molecular replacement. It was, refined at 2.1 A resolution to an R value of 18.4%, and compared with, Rhodobacter capsulatus strain M110 cytochrome c' (RCCP-M110). Although, these two proteins are very similar in sequence and structure, the, intermolecular interaction is largely different. In RCCP-M110, the, molecules dimerize through interaction of helix B to form an antiparallel, arrangement. When crystallized in the presence of Zn ions, molecules of, RCCP-SL were found to be arranged as linear polymers connected by the, bridging Zn ions. The changes in conformation of the side chains induced, by binding of the Zn ions, by the substitution of Glu90 for Asp90, and by, the different arrangement of the molecules, are discussed in detail.
About this Structure
1CPR is a Single protein structure of sequence from Rhodobacter capsulatus with ZN and HEM as ligands. Full crystallographic information is available from OCA.
Reference
Structure of cytochrome c' from Rhodobacter capsulatus strain St Louis: an unusual molecular association induced by bridging Zn ions., Tahirov TH, Misaki S, Meyer TE, Cusanovich MA, Higuchi Y, Yasuoka N, Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):658-64. PMID:15299853
Page seeded by OCA on Tue Nov 20 12:39:26 2007
