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1852433 
Journal Article 
The crystallographic structure of Na,K-ATPase N-domain at 2.6 A resolution 
Hakansson, KO 
2003 
Yes 
Journal of Molecular Biology
ISSN: 0022-2836
EISSN: 1089-8638 
332 
5 
1175-1182 
English 
14499619 
WOS:000185575300018 
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. 
Na,K-ATPase structure; crystallography; HisTag; ATP binding; membrane protein