4uxv

Cytoplasmic domain of bacterial cell division protein EzrA

spinqualitylabelsall models 4uxv, resolution 3.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uxv is a 1 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.961Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EZRA_BACSU Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization. Publication Abstract from PubMed Bacterial cell division is facilitated by a molecular machine-the divisome-that assembles at mid-cell in dividing cells. The formation of the cytokinetic Z-ring by the tubulin homologue FtsZ is regulated by several factors, including the divisome component EzrA. Here we describe the structure of the 60-kDa cytoplasmic domain of EzrA, which comprises five linear repeats of an unusual triple helical bundle. The EzrA structure is bent into a semicircle, providing the protein with the potential to interact at both N- and C-termini with adjacent membrane-bound divisome components. We also identify at least two binding sites for FtsZ on EzrA and map regions of EzrA that are responsible for regulating FtsZ assembly. The individual repeats, and their linear organization, are homologous to the spectrin proteins that connect actin filaments to the membrane in eukaryotes, and we thus propose that EzrA is the founding member of the bacterial spectrin family. Structure and function of a spectrin-like regulator of bacterial cytokinesis.,Cleverley RM, Barrett JR, Basle A, Bui NK, Hewitt L, Solovyova A, Xu ZQ, Daniel RA, Dixon NE, Harry EJ, Oakley AJ, Vollmer W, Lewis RJ Nat Commun. 2014 Nov 18;5:5421. doi: 10.1038/ncomms6421. PMID:25403286 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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