1cfm: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cfm RCSB], [http://www.ebi.ac.uk/pdbsum/1cfm PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cfm RCSB], [http://www.ebi.ac.uk/pdbsum/1cfm PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CYF_CHLRE CYF_CHLRE]] 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.[HAMAP-Rule:MF_00610] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 21:11, 24 December 2014
CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTIICYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII
Structural highlights
Function[CYF_CHLRE] 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.[HAMAP-Rule:MF_00610] 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 PubMedA truncated form of cytochrome f from Chlamydomonas reinhardtii (an important eukaryotic model organism for photosynthetic electron transfer studies) has been crystallized (space group P2(1)2(1)2(1); three molecules/asymmetric unit) and its structure determined to 2.0 A resolution by molecular replacement using the coordinates of a truncated turnip cytochrome f as a model. The structure displays the same folding and detailed features as turnip cytochrome f, including (a) an unusual heme Fe ligation by the alpha-amino group of tyrosine 1, (b) a cluster of lysine residues (proposed docking site of plastocyanin), and (c) the presence of a chain of seven water molecules bound to conserved residues and extending between the heme pocket and K58 and K66 at the lysine cluster. For this array of waters, we propose a structural role. Two cytochrome f molecules are related by a noncrystallographic symmetry operator which is a distorted proper 2-fold rotation. This may represent the dimeric relation of the monomers in situ; however, the heme orientation suggested by this model is not consistent with previous EPR measurements on oriented membranes. X-ray structure of a truncated form of cytochrome f from chlamydomonas reinhardtii.,Chi YI, Huang LS, Zhang Z, Fernandez-Velasco JG, Berry EA Biochemistry. 2000 Jul 4;39(26):7689-701. PMID:10869174[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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