2VOY

CryoEM model of CopA, the copper transporting ATPase from Archaeoglobus fulgidus

Summary for 2VOY

• Entry DOI: 10.2210/pdb2voy/pdb
• EMDB information: 5004 5005
• Descriptor: POTENTIAL COPPER-TRANSPORTING ATPASE, CATION-TRANSPORTING ATPASE, SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1, ... (12 entities in total)
• Functional Keywords: hydrolasep-type atpase, cryo-em, helical reconstruction, membrane protein, copper transporter, metal binding domain, hydrolase
• Biological source: BACILLUS SUBTILIS; More
• Total number of polymer chains: 12
• Total formula weight: 75300.76

Authors

Wu, C.-C.,Rice, W.J.,Stokes, D.L. (deposition date: 2008-02-25, release date: 2009-05-26, Last modification date: 2024-10-23)

Primary citation

Wu, C.-C.,Rice, W.J.,Stokes, D.L.
Structure of a Copper Pump Suggests a Regulatory Role for its Metal-Binding Domain.
Structure, 16:976-, 2008

PubMed Abstract: P-type ATPases play an important role in Cu homeostasis, which provides sufficient Cu for metalloenzyme biosynthesis but prevents oxidative damage of free Cu to the cell. The P(IB) group of P-type ATPases includes ATP-dependent pumps of Cu and other transition metal ions, and it is distinguished from other family members by the presence of N-terminal metal-binding domains (MBD). We have determined structures of two constructs of a Cu pump from Archaeoglobus fulgidus (CopA) by cryoelectron microscopy of tubular crystals, which reveal the overall architecture and domain organization of the molecule. By comparing these structures, we localized its N-terminal MBD within the cytoplasmic domains that use ATP hydrolysis to drive the transport cycle. We have built a pseudoatomic model by fitting existing crystallographic structures into the cryoelectron microscopy maps for CopA, which suggest a Cu-dependent regulatory role for the MBD.

PubMed: 18547529
DOI: 10.1016/J.STR.2008.02.025

Experimental method

ELECTRON MICROSCOPY (18 Å)