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[[Image:1f1c.jpg|left|200px]]
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{{STRUCTURE_1f1c|  PDB=1f1c  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF CYTOCHROME C549'''


==CRYSTAL STRUCTURE OF CYTOCHROME C549==
<StructureSection load='1f1c' size='340' side='right'caption='[[1f1c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f1c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Limnospira_maxima Limnospira 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 [https://proteopedia.org/fgij/fg.htm?mol=1F1C FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1c OCA], [https://pdbe.org/1f1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f1c RCSB], [https://www.ebi.ac.uk/pdbsum/1f1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f1c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CY550_LIMMA CY550_LIMMA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f1/1f1c_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f1c ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome 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.


==Overview==
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<ref>PMID:11478889</ref>
Cytochrome 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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1F1C is a [[Single protein]] structure of 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].
</div>
<div class="pdbe-citations 1f1c" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11478889 11478889]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
[[Category: Arthrospira maxima]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Kerfeld, C A.]]
__TOC__
[[Category: Krogmann, D W.]]
</StructureSection>
[[Category: Sawaya, M R.]]
[[Category: Large Structures]]
[[Category: Yeates, T O.]]
[[Category: Limnospira maxima]]
[[Category: Dimeric cytochrome]]
[[Category: Kerfeld CA]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:46:29 2008''
[[Category: Krogmann DW]]
[[Category: Sawaya MR]]
[[Category: Yeates TO]]

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