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| | <StructureSection load='1ci3' size='340' side='right'caption='[[1ci3]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1ci3' size='340' side='right'caption='[[1ci3]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ci3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phola Phola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CI3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1CI3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ci3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phormidium_laminosum Phormidium laminosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CI3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PETA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32059 PHOLA])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ci3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ci3 OCA], [http://pdbe.org/1ci3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ci3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ci3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ci3 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ci3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ci3 OCA], [https://pdbe.org/1ci3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ci3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ci3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ci3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYF_PHOLA CYF_PHOLA]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). | + | [https://www.uniprot.org/uniprot/CYF_PHOLA CYF_PHOLA] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phola]] | + | [[Category: Phormidium laminosum]] |
| - | [[Category: Bendall, D S]] | + | [[Category: Bendall DS]] |
| - | [[Category: Carrell, C J]] | + | [[Category: Carrell CJ]] |
| - | [[Category: Cramer, W A]] | + | [[Category: Cramer WA]] |
| - | [[Category: Howe, C J]] | + | [[Category: Howe CJ]] |
| - | [[Category: Schlarb, B G]] | + | [[Category: Schlarb BG]] |
| - | [[Category: Smith, J L]] | + | [[Category: Smith JL]] |
| - | [[Category: Complex subunit]]
| + | |
| - | [[Category: Electron transfer protein]]
| + | |
| - | [[Category: Electron transport]]
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| Structural highlights
Function
CYF_PHOLA Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity).
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
Cytochrome f from the photosynthetic cytochrome b(6)f complex is unique among c-type cytochromes in its fold and heme ligation. The 1. 9-A crystal structure of the functional, extrinsic portion of cytochrome f from the thermophilic cyanobacterium Phormidium laminosum demonstrates that an unusual buried chain of five water molecules is remarkably conserved throughout the biological range of cytochrome f from cyanobacteria to plants [Martinez et al. (1994) Structure 2, 95-105]. Structure and sequence conservation of the cytochrome f extrinsic portion is concentrated at the heme, in the buried water chain, and in the vicinity of the transmembrane helix anchor. The electrostatic surface potential is variable, so that the surface of P. laminosum cytochrome f is much more acidic than that from turnip. Cytochrome f is unrelated to cytochrome c(1), its functional analogue in the mitochondrial respiratory cytochrome bc(1) complex, although other components of the b(6)f and bc(1) complexes are homologous. Identical function of the two complexes is inferred for events taking place at sites of strong sequence conservation. Conserved sites throughout the entire cytochrome b(6)f/bc(1) family include the cluster-binding domain of the Rieske protein and the heme b and quinone-binding sites on the electrochemically positive side of the membrane within the b cytochrome, but not the putative quinone-binding site on the electrochemically negative side.
Structure of the soluble domain of cytochrome f from the cyanobacterium Phormidium laminosum.,Carrell CJ, Schlarb BG, Bendall DS, Howe CJ, Cramer WA, Smith JL Biochemistry. 1999 Jul 27;38(30):9590-9. PMID:10423236[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Carrell CJ, Schlarb BG, Bendall DS, Howe CJ, Cramer WA, Smith JL. Structure of the soluble domain of cytochrome f from the cyanobacterium Phormidium laminosum. Biochemistry. 1999 Jul 27;38(30):9590-9. PMID:10423236 doi:10.1021/bi9903190
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