2JEE

Xray structure of E. coli YiiU

Summary for 2JEE

• Entry DOI: 10.2210/pdb2jee/pdb
• Descriptor: CELL DIVISION PROTEIN ZAPB (2 entities in total)
• Functional Keywords: ftsz, septum, coiled-coil, cell division, cell cycle, hypothetical protein
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm: P0AF36
• Total number of polymer chains: 4
• Total formula weight: 38583.12

Authors

Moller-Jensen, J.,Gerdes, K.,Lowe, J. (deposition date: 2007-01-16, release date: 2008-02-05, Last modification date: 2024-05-08)

Primary citation

Ebersbach, G.,Galli, E.,Moller-Jensen, J.,Lowe, J.,Gerdes, K.
Novel Coiled-Coil Cell Division Factor Zapb Stimulates Z Ring Assembly and Cell Division.
Mol.Microbiol., 68:720-, 2008

PubMed Abstract: Formation of the Z ring is the first known event in bacterial cell division. However, it is not yet known how the assembly and contraction of the Z ring are regulated. Here, we identify a novel cell division factor ZapB in Escherichia coli that simultaneously stimulates Z ring assembly and cell division. Deletion of zapB resulted in delayed cell division and the formation of ectopic Z rings and spirals, whereas overexpression of ZapB resulted in nucleoid condensation and aberrant cell divisions. Localization of ZapB to the divisome depended on FtsZ but not FtsA, ZipA or FtsI, and ZapB interacted with FtsZ in a bacterial two-hybrid analysis. The simultaneous inactivation of FtsA and ZipA prevented Z ring assembly and ZapB localization. Time lapse microscopy showed that ZapB-GFP is present at mid-cell in a pattern very similar to that of FtsZ. Cells carrying a zapB deletion and the ftsZ84(ts) allele exhibited a synthetic sick phenotype and aberrant cell divisions. The crystal structure showed that ZapB exists as a dimer that is 100% coiled-coil. In vitro, ZapB self-assembled into long filaments and bundles. These results raise the possibility that ZapB stimulates Z ring formation directly via its capacity to self-assemble into larger structures.

PubMed: 18394147
DOI: 10.1111/J.1365-2958.2008.06190.X

Experimental method

X-RAY DIFFRACTION (2.8 Å)