1m56: Difference between revisions
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|PDB= 1m56 |SIZE=350|CAPTION= <scene name='initialview01'>1m56</scene>, resolution 2.3Å | |PDB= 1m56 |SIZE=350|CAPTION= <scene name='initialview01'>1m56</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEH:DI-STEAROYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEH</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1m57|1M57]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m56 OCA], [http://www.ebi.ac.uk/pdbsum/1m56 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m56 RCSB]</span> | |||
}} | }} | ||
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[[Category: Svensson-Ek, M.]] | [[Category: Svensson-Ek, M.]] | ||
[[Category: Tornroth, S.]] | [[Category: Tornroth, S.]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
''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 22:11:25 2008'' | ||
Revision as of 22:11, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Activity: | Cytochrome-c oxidase, with EC number 1.9.3.1 | ||||||
| Related: | 1M57
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)
OverviewOverview
The structure of cytochrome c oxidase from Rhodobacter sphaeroides has been solved at 2.3/2.8A (anisotropic resolution). This high-resolution structure revealed atomic details of a bacterial terminal oxidase including water molecule positions and a potential oxygen pathway, which has not been reported in other oxidase structures. A comparative study of the wild-type and the EQ(I-286) mutant enzyme revealed structural rearrangements around E(I-286) that could be crucial for proton transfer in this enzyme. In the structure of the mutant enzyme, EQ(I-286), which cannot transfer protons during oxygen reduction, the side-chain of Q(I-286) does not have the hydrogen bond to the carbonyl oxygen of M(I-107) that is seen in the wild-type structure. Furthermore, the Q(I-286) mutant has a different arrangement of water molecules and residues in the vicinity of the Q side-chain. These differences between the structures could reflect conformational changes that take place upon deprotonation of E(I-286) during turnover of the wild-type enzyme, which could be part of the proton-pumping machinery of the enzyme.
About this StructureAbout this Structure
1M56 is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.
ReferenceReference
The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides., Svensson-Ek M, Abramson J, Larsson G, Tornroth S, Brzezinski P, Iwata S, J Mol Biol. 2002 Aug 9;321(2):329-39. PMID:12144789
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