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Structure. 2011 Sep 7;19(9):1219-32. doi: 10.1016/j.str.2011.05.014. Epub 2011 Aug 4.

The architecture of CopA from Archeaoglobus fulgidus studied by cryo-electron microscopy and computational docking.

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1
Skirball Institute, New York University School of Medicine, New York, NY 10016, USA.

Abstract

CopA uses ATP to pump Cu(+) across cell membranes. X-ray crystallography has defined atomic structures of several related P-type ATPases. We have determined a structure of CopA at 10 Å resolution by cryo-electron microscopy of a new crystal form and used computational molecular docking to study the interactions between the N-terminal metal-binding domain (NMBD) and other elements of the molecule. We found that the shorter-chain lipids used to produce these crystals are associated with movements of the cytoplasmic domains, with a novel dimer interface and with disordering of the NMBD, thus offering evidence for the transience of its interaction with the other cytoplasmic domains. Docking identified a binding site that matched the location of the NMBD in our previous structure by cryo-electron microscopy, allowing a more detailed view of its binding configuration and further support for its role in autoinhibition.

PMID:
21820315
PMCID:
PMC3168071
DOI:
10.1016/j.str.2011.05.014
[Indexed for MEDLINE]
Free PMC Article
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