1E29
PSII associated cytochrome C549 from Synechocystis sp.
Summary for 1E29
| Entry DOI | 10.2210/pdb1e29/pdb |
| Descriptor | CYTOCHROME C549, HEME C, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | electron transport, psii associated cytochrome, cytochrome, low potential, bis_histidinyl, psii modulator |
| Biological source | SYNECHOCYSTIS SP |
| Total number of polymer chains | 1 |
| Total formula weight | 15873.44 |
| Authors | Frazao, C.,Enguita, F.J.,Coelho, R.,Sheldrick, G.M. (deposition date: 2000-05-19, release date: 2001-05-04, Last modification date: 2024-11-06) |
| Primary citation | Frazao, C.,Enguita, F.J.,Coelho, R.,Sheldrick, G.M.,Navarro, J.A.,Hervas, M.,De La Rosa, M.A.,Carrondo, M.A. Crystal Structure of Low-Potential Cytochrome C549 from Synechocystis Sp. Pcc 6803 at 1.21A Resolution J.Biol.Inorg.Chem., 6:324-, 2001 Cited by PubMed Abstract: 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. PubMed: 11315568DOI: 10.1007/S007750100208 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.21 Å) |
Structure validation
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