1f7x
SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA
|
OverviewOverview
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 A for the backbone atoms, 0. 78 +/-, 0.05 A for all atoms, and 0.45 +/- 0.04 A 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-terminal 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.
About this StructureAbout this Structure
1F7X is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of ZipA, a crucial component of Escherichia coli cell division., Moy FJ, Glasfeld E, Mosyak L, Powers R, Biochemistry. 2000 Aug 8;39(31):9146-56. PMID:10924108
Page seeded by OCA on Tue Nov 20 14:41:31 2007