3J09

High resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA

Summary for 3J09

• Entry DOI: 10.2210/pdb3j09/pdb
• EMDB information: 5004 5271
• Descriptor: copper-exporting P-type ATPase A (1 entity in total)
• Functional Keywords: p-type atpase, copper transporter, copa, adenosine triphosphatases, archaeal proteins, cation transport proteins, cryoelectron microscopy, hydrolase, metal transport
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 2
• Total formula weight: 155631.30

Authors

Wu, C.,Allen, G.S.,Cardozo, T.,Stokes, D.L. (deposition date: 2011-05-09, release date: 2011-08-24, Last modification date: 2024-02-21)

Primary citation

Allen, G.S.,Wu, C.C.,Cardozo, T.,Stokes, D.L.
The Architecture of CopA from Archeaoglobus fulgidus Studied by Cryo-Electron Microscopy and Computational Docking.
Structure, 19:1219-1232, 2011

PubMed 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.

PubMed: 21820315
DOI: 10.1016/j.str.2011.05.014

Experimental method

ELECTRON MICROSCOPY (10 Å)