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

ABSTRACT: 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-subunit in complex with ADP. These structural data suggest a new mechanism of F1F0-ATPase regulation in α-proteobacteria.

SUBMITTER: Serrano P 

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

REPOSITORIES: biostudies-literature