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4UXV

Cytoplasmic domain of bacterial cell division protein EzrA

Summary for 4UXV
Entry DOI10.2210/pdb4uxv/pdb
Related4UY3
DescriptorSEPTATION RING FORMATION REGULATOR EZRA (1 entity in total)
Functional Keywordscell cycle, divisome, ftsz, cell wall, tubulin, spectrin, z-ring
Biological sourceBACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168
Cellular locationCell membrane; Single-pass membrane protein: O34894
Total number of polymer chains1
Total formula weight63171.11
Authors
Cleverley, R.M.,Barrett, J.R.,Basle, A.,Khai-Bui, N.,Hewitt, L.,Solovyova, A.,Xu, Z.,Daniela, R.A.,Dixon, N.E.,Harry, E.J.,Oakley, A.J.,Vollmer, W.,Lewis, R.J. (deposition date: 2014-08-27, release date: 2014-10-22, Last modification date: 2024-05-08)
Primary citationCleverley, R.M.,Barrett, J.R.,Basle, A.,Bui, N.K.,Hewitt, L.,Solovyova, A.,Xu, Z.,Daniel, R.A.,Dixon, N.E.,Harry, E.J.,Oakley, A.J.,Vollmer, W.,Lewis, R.J.
Structure and Function of a Spectrin-Like Regulator of Bacterial Cytokinesis.
Nat.Commun., 5:5421-, 2014
Cited by
PubMed Abstract: 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.
PubMed: 25403286
DOI: 10.1038/NCOMMS6421
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.961 Å)
Structure validation

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