AI Article Synopsis
- The N-domain of porcine alpha(2) Na,K-ATPase was crystallized and its structure resolved to a high resolution of 2.6A using mercury compounds and synchrotron data.
- The domain features a seven-stranded antiparallel beta-sheet, with an additional hairpin and five alpha-helices contributing to its structure.
- A significant overlap (75%) was observed with the Ca-ATPase N-domain, and the study discusses key residues related to hydrophobicity and charge, also including a hexahistidine tag binding to nickel ions.
Article 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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| http://dx.doi.org/10.1016/j.jmb.2003.07.012 | DOI Listing |
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