2MRW
Solution Structure of MciZ from Bacillus subtilis
Summary for 2MRW
| Entry DOI | 10.2210/pdb2mrw/pdb |
| NMR Information | BMRB: 25096 |
| Descriptor | Cell division factor (1 entity in total) |
| Functional Keywords | ftsz, cell cycle |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 1 |
| Total formula weight | 4785.78 |
| Authors | Castellen, P.,Sforca, M.L.,Zeri, A.C.M.,Gueiros-Filho, F.J. (deposition date: 2014-07-16, release date: 2015-03-25, Last modification date: 2024-05-01) |
| Primary citation | Bisson-Filho, A.W.,Discola, K.F.,Castellen, P.,Blasios, V.,Martins, A.,Sforca, M.L.,Garcia, W.,Zeri, A.C.,Erickson, H.P.,Dessen, A.,Gueiros-Filho, F.J. FtsZ filament capping by MciZ, a developmental regulator of bacterial division. Proc.Natl.Acad.Sci.USA, 112:E2130-E2138, 2015 Cited by PubMed Abstract: Cytoskeletal structures are dynamically remodeled with the aid of regulatory proteins. FtsZ (filamentation temperature-sensitive Z) is the bacterial homolog of tubulin that polymerizes into rings localized to cell-division sites, and the constriction of these rings drives cytokinesis. Here we investigate the mechanism by which the Bacillus subtilis cell-division inhibitor, MciZ (mother cell inhibitor of FtsZ), blocks assembly of FtsZ. The X-ray crystal structure reveals that MciZ binds to the C-terminal polymerization interface of FtsZ, the equivalent of the minus end of tubulin. Using in vivo and in vitro assays and microscopy, we show that MciZ, at substoichiometric levels to FtsZ, causes shortening of protofilaments and blocks the assembly of higher-order FtsZ structures. The findings demonstrate an unanticipated capping-based regulatory mechanism for FtsZ. PubMed: 25848052DOI: 10.1073/pnas.1414242112 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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