Solution structure of ZipA, a crucial component of Escherichia coli cell division

被引:47
作者
Moy, FJ
Glasfeld, E
Mosyak, L
Powers, R
机构
[1] Wyeth Res, Dept Biol Chem, Cambridge, MA 02140 USA
[2] Wyeth Res, Dept Infect Dis, Pearl River, NY 10965 USA
关键词
D O I
10.1021/bi0009690
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
ZipA, an essential component of cell division in Escherichia coli, interacts with the FtsZ protein at the midcell in one of the initial steps of septum formation, The high-resolution solution structure of the 144-residue C-terminal domain of E. coli ZipA (ZiPA(185-328)) has been determined by multidimensional heteronuclear NMR. A total of 30 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of 2758 experimental NMR restraints. The atomic root means square distribution about the mean coordinate positions for residues 6-142 for the 30 structures is 0.37 +/- 0.04 Angstrom for the backbone atoms, 0.78 +/- 0.05 Angstrom for all atoms, and 0.45 +/- 0.04 Angstrom, for all atoms excluding disordered side chains. The NMR solution structure of ZiPA(185-328) is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands where the alpha-helices and the beta-sheet form surfaces directly opposite each other. A C-tenninal peptide from FtsZ has been shown to bind ZiPA(185-328) in a hydrophobic channel formed by the beta-sheet providing insight into the ZipA-FtsZ interaction. An unexpected similarity between the ZiPA(185-328) fold and the split beta-alpha-beta fold observed in many RNA binding proteins may further our understanding of the critical ZipA-FtsZ interaction.
引用
收藏
页码:9146 / 9156
页数:11
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