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NMR structures of ?-proteobacterial ATPase-regulating ?-subunits.


ABSTRACT: NMR structures of ?-subunits, which are recently discovered ?-proteobacterial F1F0-ATPase-regulatory proteins representing a Pfam protein family of 246 sequences from 219 species (PF07345), exhibit a four-helix bundle, which is different from all other known F1F0-ATPase inhibitors. Chemical shift mapping reveals a conserved ADP/ATP binding site in ?-subunit, which mediates long-range conformational changes related to function, as revealed by the structure of the Paracoccus denitrificans ?-subunit in complex with ADP. These structural data suggest a new mechanism of F1F0-ATPase regulation in ?-proteobacteria.

SUBMITTER: Serrano P 

PROVIDER: S-EPMC4089900 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature

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NMR structures of α-proteobacterial ATPase-regulating ζ-subunits.

Serrano Pedro P   Geralt Michael M   Mohanty Biswaranjan B   Wüthrich Kurt K  

Journal of molecular biology 20140513 14


NMR structures of ζ-subunits, which are recently discovered α-proteobacterial F1F0-ATPase-regulatory proteins representing a Pfam protein family of 246 sequences from 219 species (PF07345), exhibit a four-helix bundle, which is different from all other known F1F0-ATPase inhibitors. Chemical shift mapping reveals a conserved ADP/ATP binding site in ζ-subunit, which mediates long-range conformational changes related to function, as revealed by the structure of the Paracoccus denitrificans ζ-subuni  ...[more]

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