From static structure to living protein: computational analysis of cytochrome c oxidase main-chain flexibility.

ABSTRACT: Crystallographic structure and deuterium accessibility comparisons of CcO in different redox states have suggested conformational changes of mechanistic significance. To predict the intrinsic flexibility and low energy motions in CcO, this work has analyzed available high-resolution crystallographic structures with ProFlex and elNémo computational methods. The results identify flexible regions and potential conformational changes in CcO that correlate well with published structural and biochemical data and provide mechanistic insights. CcO is predicted to undergo rotational motions on the interior and exterior of the membrane, driven by transmembrane helical tilting and bending, coupled with rocking of the β-sheet domain. Consequently, the proton K-pathway becomes sufficiently flexible for

SUBMITTER: Buhrow L 

PROVIDER: S-EPMC3341565 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature