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J Mol Biol. 2014 Jul 15;426(14):2547-53. doi: 10.1016/j.jmb.2014.05.004. Epub 2014 May 13.

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

Author information

1
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA; Joint Center for Structural Genomics (http://www.jcsg.org.), La Jolla, CA 92037, USA. Electronic address: serrano@scripps.edu.
2
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA; Joint Center for Structural Genomics (http://www.jcsg.org.), La Jolla, CA 92037, USA.
3
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA; Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA; Joint Center for Structural Genomics (http://www.jcsg.org.), La Jolla, CA 92037, USA.

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.

KEYWORDS:

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

PMID:
24838125
PMCID:
PMC4089900
DOI:
10.1016/j.jmb.2014.05.004
[Indexed for MEDLINE]
Free PMC Article

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