1Q3I

The Crystallographic Structure of Na,K-ATPase N-domain at 2.6 A Resolution

(2003) J Mol Biol 332: 1175-1182

• PubMed: 14499619 Search on PubMed
• DOI: https://doi.org/10.1016/j.jmb.2003.07.012
• Primary Citation of Related Structures:  
  1Q3I


• PubMed Abstract: 
  

  The structure of the N-domain of porcine alpha(2) Na,K-ATPase was determined crystallographically to 3.2A resolution by isomorphous heavy-atom replacement using a single mercury derivative. The structure was finally refined against 2.6A resolution synchrotron data. The domain forms a seven-stranded antiparallel beta-sheet with two additional beta-strands forming a hairpin and five alpha-helices. Approximately 75% of the residues were superimposable with residues from the structure of Ca-ATPase N-domain, and a structure-based sequence alignment is presented. The positions of key residues are discussed in relation to the pattern of hydrophobicity, charge and sequence conservation of the molecular surface. The structure of a hexahistidine tag binding to nickel ions is presented.

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Organizational Affiliation: 

August Krogh Institute, Copenhagen University, Universitetsparken 13, DK-2100 OE, Copenhagen, Denmark. kohakansson@aki.ku.dk