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

Pedro Serrano, Michael Geralt, Biswaranjan Mohanty, Kurt Wüthrich

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15 Citations (Scopus)

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 F 1F0-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.

Original languageEnglish
Pages (from-to)2547-2553
Number of pages7
JournalJournal of Molecular Biology
Volume426
Issue number14
DOIs
Publication statusPublished - 15 Jul 2014
Externally publishedYes

Keywords

  • ATPase-regulating protein
  • NMR structure determination
  • PF07345
  • α-proteobacteria
  • ζ-subunit

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