1f1c
From Proteopedia
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|PDB= 1f1c |SIZE=350|CAPTION= <scene name='initialview01'>1f1c</scene>, resolution 2.3Å | |PDB= 1f1c |SIZE=350|CAPTION= <scene name='initialview01'>1f1c</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/1f1c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f1c RCSB]</span> | ||
}} | }} | ||
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[[Category: Sawaya, M R.]] | [[Category: Sawaya, M R.]] | ||
[[Category: Yeates, T O.]] | [[Category: Yeates, T O.]] | ||
| - | [[Category: HEM]] | ||
[[Category: dimeric cytochrome]] | [[Category: dimeric cytochrome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:13:53 2008'' |
Revision as of 17:14, 30 March 2008
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| , resolution 2.3Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF CYTOCHROME C549
Overview
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
1F1C is a Single protein structure of sequence from Arthrospira maxima. Full crystallographic information is available from OCA.
Reference
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
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