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1GU2

Crystal structure of oxidized cytochrome c'' from Methylophilus methylotrophus

Summary for 1GU2
Entry DOI10.2210/pdb1gu2/pdb
Related1E8E
DescriptorCYTOCHROME C'', HEME C (3 entities in total)
Functional Keywordsoxidoreductase(cytochrome), oxidoreductase, electron transport
Biological sourceMETHYLOPHILUS METHYLOTROPHUS
Total number of polymer chains2
Total formula weight28635.99
Authors
Enguita, F.J.,Pohl, E.,Rodrigues, A.,Santos, H.,Carrondo, M.A. (deposition date: 2002-01-22, release date: 2003-01-16, Last modification date: 2024-11-13)
Primary citationEnguita, F.J.,Pohl, E.,Turner, D.L.,Santos, H.,Carrondo, M.A.
Structural Evidence for a Proton Transfer Pathway Coupled with Haem Reduction of Cytochrome C" from Methylophilus Methylotrophus.
J.Biol.Inorg.Chem., 11:189-, 2006
Cited by
PubMed Abstract: The crystal structures of the oxidized and reduced forms of cytochrome c" from Methylophilus methylotrophus were solved from X-ray synchrotron data to atomic resolution. The overall fold of the molecule in the two redox states is very similar and is comparable to that of the oxygen-binding protein from the purple phototrophic bacterium Rhodobacter sphaeroides. However, significant modifications occur near the haem group, in particular the detachment from axial binding of His95 observed upon reduction as well as the adoption of different conformations of some protonatable residues that form a possible proton path from the haem pocket to the protein surface. These changes are associated with the previously well characterized redox-Bohr behaviour of this protein. Furthermore they provide a model for one of the presently proposed mechanisms of proton translocation in the much more complex protein cytochrome c oxidase.
PubMed: 16341897
DOI: 10.1007/S00775-005-0065-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.19 Å)
Structure validation

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数据于2025-07-09公开中

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