1GU2

Crystal structure of oxidized cytochrome c'' from Methylophilus methylotrophus

Summary for 1GU2

• Entry DOI: 10.2210/pdb1gu2/pdb
• Related: 1E8E
• Descriptor: CYTOCHROME C'', HEME C (3 entities in total)
• Functional Keywords: oxidoreductase(cytochrome), oxidoreductase, electron transport
• Biological source: METHYLOPHILUS METHYLOTROPHUS
• Total number of polymer chains: 2
• Total formula weight: 28635.99

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 citation

Enguita, 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

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

Experimental method

X-RAY DIFFRACTION (1.19 Å)