1f1f: Difference between revisions
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<StructureSection load='1f1f' size='340' side='right'caption='[[1f1f]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='1f1f' size='340' side='right'caption='[[1f1f]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1f1f]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1f1f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrospira_maxima Arthrospira maxima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F1F FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand= | </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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cyi|1cyi]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cyi|1cyi]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1f OCA], [https://pdbe.org/1f1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f1f RCSB], [https://www.ebi.ac.uk/pdbsum/1f1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f1f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CYC6_ARTMA CYC6_ARTMA]] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 17:49, 3 March 2021
CRYSTAL STRUCTURE OF CYTOCHROME C6 FROM ARTHROSPIRA MAXIMACRYSTAL STRUCTURE OF CYTOCHROME C6 FROM ARTHROSPIRA MAXIMA
Structural highlights
Function[CYC6_ARTMA] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis. 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 PubMedCytochrome c(6) and cytochrome c-549 are small (89 and 130 amino acids, respectively) monoheme cytochromes that function in photosynthesis. They appear to have descended relatively recently from the same ancestral gene but have diverged to carry out very different functional roles, underscored by the large difference between their midpoint potentials of nearly 600 mV. We have determined the X-ray crystal structures of both proteins isolated from the cyanobacterium Arthrospira maxima. The two structures are remarkably similar, superimposing on backbone atoms with an rmsd of 0.7 A. Comparison of the two structures suggests that differences in solvent exposure of the heme and the electrostatic environment of the heme propionates, as well as in heme iron ligation, are the main determinants of midpoint potential in the two proteins. In addition, the crystal packing of both A. maxima cytochrome c-549 and cytochrome c(6) suggests that the proteins oligomerize. Finally, the cytochrome c-549 dimer we observe can be readily fit into the recently described model of cyanobacterial photosystem II. Structures of cytochrome c-549 and cytochrome c6 from the cyanobacterium Arthrospira maxima.,Sawaya MR, Krogmann DW, Serag A, Ho KK, Yeates TO, Kerfeld CA Biochemistry. 2001 Aug 7;40(31):9215-25. PMID:11478889[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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