1f1c: Difference between revisions
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<table><tr><td colspan='2'>[[1f1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrospira_maxima Arthrospira maxima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F1C FirstGlance]. <br> | <table><tr><td colspan='2'>[[1f1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrospira_maxima Arthrospira maxima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F1C FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=1f1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f1c RCSB], [http://www.ebi.ac.uk/pdbsum/1f1c 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=1f1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1c OCA], [http://pdbe.org/1f1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f1c RCSB], [http://www.ebi.ac.uk/pdbsum/1f1c PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1f1c" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 17:36, 10 September 2015
CRYSTAL STRUCTURE OF CYTOCHROME C549CRYSTAL STRUCTURE OF CYTOCHROME C549
Structural highlights
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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