1F7X

SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA

Summary for 1F7X

• Entry DOI: 10.2210/pdb1f7x/pdb
• Related: 1F7W
• NMR Information: BMRB: 4717
• Descriptor: CELL DIVISION PROTEIN ZIPA (1 entity in total)
• Functional Keywords: alpha-beta fold, cell division, septation, transmembrane, inner membrane, cell cycle
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Single-pass type I membrane protein: P77173
• Total number of polymer chains: 1
• Total formula weight: 16135.43

Authors

Moy, F.J.,Glasfeld, E.,Mosyak, L.,Powers, R. (deposition date: 2000-06-28, release date: 2001-06-28, Last modification date: 2024-05-22)

Primary citation

Moy, F.J.,Glasfeld, E.,Mosyak, L.,Powers, R.
Solution structure of ZipA, a crucial component of Escherichia coli cell division.
Biochemistry, 39:9146-9156, 2000

PubMed Abstract: 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.

PubMed: 10924108
DOI: 10.1021/bi0009690

Experimental method

SOLUTION NMR