Motion in Cytochrome C Oxidase, ba3 (T. Thermophilus) [CCO_tt]

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

Structures 1EHK Conformation 1 1XME 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 T Soulimane, G Buse, GP Bourenkov, HD Bartunik, R Huber, ME Than (2000). Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus. EMBO J 19(8):1766-1776 [Medline info for 10775261] LM Hunsicker-Wang, RL Pacoma, Y Chen, JA Fee, CD Stout (2005). A novel cryprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus. Acta Crystallogr D Biol Crystallogr 61:340-343 [Medline info for 15735345]

GO terms associated with structures Molecular function copper ion binding, cytochrome-c oxidase activity Cellular component 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