NMR structures of α-proteobacterial ATPase-regulating ζ-subunits.
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.
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.
Pedro
P
Serrano
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.
Michael
M
Geralt
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.
Biswaranjan
B
Mohanty
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.
Kurt
K
Wüthrich
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D020561:Alphaproteobacteria / Q000737:chemistry*; D025243:Bacterial Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010231:Paracoccus denitrificans / Q000737:chemistry; D011487:Protein Conformation; D021122:Protein Subunits
D021122:Protein Subunits; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D025243:Bacterial Proton-Translocating ATPases
ATPase-regulating protein; NMR structure determination; PF07345; α-proteobacteria; ζ-subunit