1wad
From Proteopedia
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|PDB= 1wad |SIZE=350|CAPTION= <scene name='initialview01'>1wad</scene>, resolution 1.8Å | |PDB= 1wad |SIZE=350|CAPTION= <scene name='initialview01'>1wad</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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=1wad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wad OCA], [http://www.ebi.ac.uk/pdbsum/1wad PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wad RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Sieker, L.]] | [[Category: Sieker, L.]] | ||
[[Category: Wilson, K.]] | [[Category: Wilson, K.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: HEM]] | ||
[[Category: calcium binding]] | [[Category: calcium binding]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:33:28 2008'' |
Revision as of 21:33, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYTOCHROME C3 WITH 4 HEME GROUPS AND ONE CALCIUM ION
Overview
Crystals of the tetraheme cytochrome c3 from sulfate-reducing bacteria Desulfovibrio gigas (Dg) (MW 13 kDa, 111 residues, four heme groups) were obtained and X-ray diffraction data collected to 1.8 A resolution. The structure was solved by the method of molecular replacement and the resulting model refined to a conventional R-factor of 14.9%. The three-dimensional structure shows many similarities to other known crystal structures of tetraheme c3 cytochromes, but it also shows some remarkable differences. In particular, the location of the aromatic residues around the heme groups, which may play a fundamental role in the electron transfer processes of the molecule, are well conserved in the cases of hemes I, III, and IV. However, heme II has an aromatic environment that is completely different to that found in other related cytochromes c3. Another unusual feature is the presence of a Ca2+ ion coordinated by oxygen atoms supplied by the protein within a loop near the N-terminus. It is speculated that this loop may be stabilized by the presence of this Ca2+ ion, may contribute to heme-redox perturbation, and might even be involved in the specificity of recognition with its redox partner.
About this Structure
1WAD is a Single protein structure of sequence from Desulfovibrio gigas. Full crystallographic information is available from OCA.
Reference
Cytochrome c3 from Desulfovibrio gigas: crystal structure at 1.8 A resolution and evidence for a specific calcium-binding site., Matias PM, Morais J, Coelho R, Carrondo MA, Wilson K, Dauter Z, Sieker L, Protein Sci. 1996 Jul;5(7):1342-54. PMID:8819167
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