1HF2
Crystal structure of the bacterial cell-division inhibitor MinC from T. maritima
Summary for 1HF2
| Entry DOI | 10.2210/pdb1hf2/pdb |
| Descriptor | SEPTUM SITE-DETERMINING PROTEIN MINC (2 entities in total) |
| Functional Keywords | cell division protein, ftsz, septum, bacterial cell division, beta helix |
| Biological source | THERMOTOGA MARITIMA |
| Total number of polymer chains | 4 |
| Total formula weight | 91028.08 |
| Authors | Cordell, S.C.,Anderson, R.E.,Lowe, J. (deposition date: 2000-11-27, release date: 2001-05-30, Last modification date: 2024-05-08) |
| Primary citation | Cordell, S.C.,Anderson, R.E.,Lowe, J. Crystal Structure of the Bacterial Cell-Division Inhibitor Minc Embo J., 20:2454-, 2001 Cited by PubMed Abstract: Bacterial cell division requires accurate selection of the middle of the cell, where the bacterial tubulin homologue FtsZ polymerizes into a ring structure. In Escherichia coli, site selection is dependent on MinC, MinD and MINE: MinC acts, with MinD, to inhibit division at sites other than the midcell by directly interacting with FTSZ: Here we report the crystal structure to 2.2 A of MinC from Thermotoga maritima. MinC consists of two domains separated by a short linker. The C-terminal domain is a right-handed beta-helix and is involved in dimer formation. The crystals contain two different MinC dimers, demonstrating flexibility in the linker region. The two-domain architecture and dimerization of MinC can be rationalized with a model of cell division inhibition. MinC does not act like SulA, which affects the GTPase activity of FtsZ, and the model can explain how MinC would select for the FtsZ polymer rather than the monomer. PubMed: 11350934DOI: 10.1093/EMBOJ/20.10.2454 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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