3MCD
Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factor
Summary for 3MCD
| Entry DOI | 10.2210/pdb3mcd/pdb |
| Related | 3KU7 |
| Descriptor | Cell division topological specificity factor (1 entity in total) |
| Functional Keywords | cytokinesis, mine, topological specificity factor, cell cycle, cell division |
| Biological source | Helicobacter pylori (Campylobacter pylori) |
| Total number of polymer chains | 2 |
| Total formula weight | 18431.34 |
| Authors | Kang, G.B.,Song, H.E.,Kim, M.K.,Youn, H.S.,Lee, J.G.,An, J.Y.,Jeon, H.,Chun, J.S.,Eom, S.H. (deposition date: 2010-03-29, release date: 2010-05-05, Last modification date: 2024-03-20) |
| Primary citation | Kang, G.B.,Song, H.E.,Kim, M.K.,Youn, H.S.,Lee, J.G.,An, J.Y.,Chun, J.S.,Jeon, H.,Eom, S.H. Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factor Mol.Microbiol., 76:1222-1231, 2010 Cited by PubMed Abstract: In Gram-negative bacteria, proper placement of the FtsZ ring, mediated by nucleoid occlusion and the activities of the dynamic oscillating Min proteins MinC, MinD and MinE, is required for correct positioning of the cell division septum. MinE is a topological specificity factor that counters the activity of MinCD division inhibitor at the mid-cell division site. Its structure consists of an anti-MinCD domain and a topology specificity domain (TSD). Previous NMR analysis of truncated Escherichia coli MinE showed that the TSD domain contains a long alpha-helix and two anti-parallel beta-strands, which mediate formation of a homodimeric alpha/beta structure. Here we report the crystal structure of full-length Helicobacter pylori MinE and redefine its TSD based on that structure. The N-terminal region of the TSD (residues 19-26), previously defined as part of the anti-MinCD domain, forms a beta-strand (betaA) and participates in TSD folding. In addition, H. pylori MinE forms a dimer through the interaction of anti-parallel betaA-strands. Moreover, we observed serial dimer-dimer interactions within the crystal packing, resulting in the formation of a multimeric structure. We therefore redefine the functional domain of MinE and propose that a multimeric filamentous structure is formed through anti-parallel beta-strand interactions. PubMed: 20398219DOI: 10.1111/j.1365-2958.2010.07160.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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