Motion in Cytochrome C Oxidase, aa3 (pracoccus denitrificans) [CCO_pd]

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Classification Suspected Fragment Motion, Shear Mechanism [F-s-2]

Structures 1AR1 Conformation 1 [ PartsList ] 1QLE Conformation 2

Description Cytochrome C oxidase (cytochrome aa3) from Paracoccus denitrificans contains a tightly bound Mn(2+) ion which responds to reduction of the enzyme by a change in its EPR signal. The change possibly reflects the rearrangement in the rhombic octahedral coordination environment of the central Mn(2+) atom and is indicative of a redox-linked conformational transition in the enzyme.

Particular values describing motion Creation Date = 20050816 Experimental Methods = e (X-ray crystallography) Modification Date = 2005-08-15 13:06:58.000

References S Iwata, C Ostermeier, B Ludwig, H Michel (1995). Structure at 2.8A resolution of cytochrome C Oxidase from Paracoccus denitrificans. Nature 376(6542):660-669 [Medline info for 7651515] A Harrenga, H Michel (1999). The Cytochrome C Oxidase from Paracoccus Denitrificans does not change the metal center ligation upon reduction. J.Biol.Chem 274(47):33296-33299 [Medline info for 10559205] H Michel, J Behr, A Harrenga, A Kannt (1998). Cytochrome C Oxidase: Structure and Spectroscopy. Annu. Rev. Biophys. Biomol. Struct. 27: 329-356. [Medline info for 964687]

GO terms associated with structures Molecular function copper ion binding, cytochrome-c oxidase activity Cellular component membrane, integral to membrane, inner membrane Biological process electron transport

Morphs

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Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu