Structural highlights
Function
[CY550_SYNY3] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Required for normal function or stabilization of PSII. Extrinsic protein associated with PSII that enhances oxygen evolution.
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
The crystal structure of low-potential cytochrome c549, an extrinsic component of the photosystem II (PS II) from Synechocystis sp. PCC 6803, was obtained directly from single-wavelength 1.21 A resolution diffraction data. This is the first monodomain bis-histidinyl monoheme cytochrome c to be structurally characterized. The extended N-terminal region of c549 builds up a two-strand antiparallel beta-sheet in a hairpin motif, which extends through two molecules owing to crystal packing. Both peptide termini are involved in crystal contacts, which may explain their protrusion out of the globular fold. The C-terminus is preceded by a 9 A-long hydrophobic finger extending from a positively charged base and could be involved in PSII interactions, as well as a protruding negative patch built by a set of conserved acidic residues among c549 sequences.
Crystal structure of low-potential cytochrome c549 from Synechocystis sp. PCC 6803 at 1.21 A resolution.,Frazao C, Enguita FJ, Coelho R, Sheldrick GM, Navarro JA, Hervas M, De la Rosa MA, Carrondo MA J Biol Inorg Chem. 2001 Mar;6(3):324-32. PMID:11315568[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Frazao C, Enguita FJ, Coelho R, Sheldrick GM, Navarro JA, Hervas M, De la Rosa MA, Carrondo MA. Crystal structure of low-potential cytochrome c549 from Synechocystis sp. PCC 6803 at 1.21 A resolution. J Biol Inorg Chem. 2001 Mar;6(3):324-32. PMID:11315568
