Solution Structure of ZipA, a Crucial Component of Escherichia coli Cell Division
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- 作者：Franklin J. Moy ; Elizabeth Glasfeld ; Lidia Mosyak ; and Robert Powers
- 刊名：Biochemistry
- 出版年：2000
- 出版时间：August 8, 2000
- 年：2000
- 卷：39
- 期：31
- 页码：9146 - 9156
- 全文大小：625K
- 年卷期：v.39,no.31(August 8, 2000)
- ISSN：1520-4995
文摘
ZipA, an essential component of cell division in Escherichia coli, interacts with the FtsZprotein at the midcell in one of the initial steps of septum formation. The high-resolution solution structureof the 144-residue C-terminal domain of E. coli ZipA (ZipA185-328) has been determined bymultidimensional heteronuclear NMR. A total of 30 structures were calculated by means of hybrid distancegeometry-simulated annealing using a total of 2758 experimental NMR restraints. The atomic root meanssquare distribution about the mean coordinate positions for residues 6-142 for the 30 structures is 0.37± 0.04 Å for the backbone atoms, 0.78 ± 0.05 Å for all atoms, and 0.45 ± 0.04 Å for all atoms excludingdisordered side chains. The NMR solution structure of ZipA185-328 is composed of three 
-helices and a
-sheet consisting of six antiparallel -strands where the -helices and the -sheet form surfaces directlyopposite each other. A C-terminal peptide from FtsZ has been shown to bind ZipA185-328 in a hydrophobicchannel formed by the -sheet providing insight into the ZipA-FtsZ interaction. An unexpected similaritybetween the ZipA185-328 fold and the split -- fold observed in many RNA binding proteins mayfurther our understanding of the critical ZipA-FtsZ interaction.
-helices and a-sheet consisting of six antiparallel -strands where the -helices and the -sheet form surfaces directlyopposite each other. A C-terminal peptide from FtsZ has been shown to bind ZipA185-328 in a hydrophobicchannel formed by the -sheet providing insight into the ZipA-FtsZ interaction. An unexpected similaritybetween the ZipA185-328 fold and the split -- fold observed in many RNA binding proteins mayfurther our understanding of the critical ZipA-FtsZ interaction.