Structural highlights
Function
[CYCP_RHOCA] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tahirov TH, Misaki S, Meyer TE, Cusanovich MA, Higuchi Y, Yasuoka N. Structure of cytochrome c' from Rhodobacter capsulatus strain St Louis: an unusual molecular association induced by bridging Zn ions. Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):658-64. PMID:15299853 doi:http://dx.doi.org/10.1107/S0907444997005805
