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

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          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.

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          Author and article information

          Journal
          Structure
          Structure (London, England : 1993)
          Elsevier BV
          1878-4186
          0969-2126
          Sep 07 2011
          : 19
          : 9
          Affiliations
          [1 ] Skirball Institute, New York University School of Medicine, New York, NY 10016, USA.
          Article
          S0969-2126(11)00241-3 NIHMS313322
          10.1016/j.str.2011.05.014
          3168071
          21820315
          1dce8248-0b84-471e-96cd-a37300976ed3
          Copyright © 2011 Elsevier Ltd. All rights reserved.
          History

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