The crystallographic structure of Na,K-ATPase N-domain at 2.6 A resolution

被引：45

作者：

Håkansson, KO ^{[1
]}

机构：

[1] Univ Copenhagen, August Krogh Inst, DK-2100 Copenhagen OE, Denmark

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2003年 / 332卷 / 05期

关键词：

Na; K-ATPase structure; crystallography; HisTag; ATP binding; membrane protein;

D O I：

10.1016/j.jmb.2003.07.012

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The structure of the N-domain of. porcine alpha(2) Na,K-ATPase was determined crystallographically to 3.2 Angstrom resolution by isomorphous heavy-atom replacement using a single mercury derivative. The structure was finally refined against 2.6 Angstrom 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. (C) 2003 Elsevier Ltd. All rights reserved.

引用

页码：1175 / 1182

页数：8

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