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| | ==Structure of the C-terminal domain of E. coli MinC at 3.0 angstrom resolution== | | ==Structure of the C-terminal domain of E. coli MinC at 3.0 angstrom resolution== |
| - | <StructureSection load='5xdm' size='340' side='right' caption='[[5xdm]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='5xdm' size='340' side='right'caption='[[5xdm]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xdm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco55 Eco55]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XDM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XDM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xdm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XDM FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">minC, b1176, JW1165 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585055 ECO55])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.004Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xdm OCA], [http://pdbe.org/5xdm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xdm RCSB], [http://www.ebi.ac.uk/pdbsum/5xdm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xdm ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xdm OCA], [https://pdbe.org/5xdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xdm RCSB], [https://www.ebi.ac.uk/pdbsum/5xdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xdm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MINC_ECOLI MINC_ECOLI]] Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.<ref>PMID:22380631</ref> | + | [https://www.uniprot.org/uniprot/MINC_ECOLI MINC_ECOLI] Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.<ref>PMID:22380631</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eco55]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Shen, Q]] | + | [[Category: Large Structures]] |
| - | [[Category: Yang, S]] | + | [[Category: Shen Q]] |
| - | [[Category: Zheng, J]] | + | [[Category: Yang S]] |
| - | [[Category: Beta helical]] | + | [[Category: Zheng J]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell division inhibition]]
| + | |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: P4322]]
| + | |
| Structural highlights
Function
MINC_ECOLI Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.[1]
Publication Abstract from PubMed
Proper cell division at the mid-site of Gram-negative bacteria reflects stringent regulation by the min system (MinC, MinD and MinE). Herein we report crystal structure of the C-terminal domain of MinC from Escherichia coli (EcMinCCTD). The MinCCTD beta helical domain is engaged in a tight homodimer, similar to Thermotoga maritima MinCCTD (TmMinCCTD). However, both EcMinCCTD and TmMinCCTD lack an alpha-helix (helix3) at their C-terminal tail, in comparison to Aquifex aerolicu MinCCTD (AaMinCCTD) which forms an extra interaction interface with MinD. To understand the role of this extra binding element in MinC/MinD interactions, we fused this helix (Aahelix3) to the C-terminus of EcMinC and examined its effect on cell morphology and cell growth. Our results revealed that Aahelix3 impaired normal cell division in vivo. Furthermore, results of a co-pelleting assay and binding free energy calculation suggested that Aahelix3 plays an essential role in AaMinCD complex formation, under the circumstance of lacking MinE in A. aerolicu. Combining these results with sequence analysis of MinC and MinD in different organisms, we propose an evolutionary relationship to rationalize different mechanisms in cell division positioning in various organisms.
Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division.,Yang S, Shen Q, Wang S, Song C, Lei Z, Han S, Zhang X, Zheng J, Jia Z Sci Rep. 2017 Aug 8;7(1):7627. doi: 10.1038/s41598-017-08213-5. PMID:28790446[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li G, Young KD. Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli. Mol Microbiol. 2012 Apr;84(2):276-95. doi: 10.1111/j.1365-2958.2012.08021.x. Epub, 2012 Mar 8. PMID:22380631 doi:10.1111/j.1365-2958.2012.08021.x
- ↑ Yang S, Shen Q, Wang S, Song C, Lei Z, Han S, Zhang X, Zheng J, Jia Z. Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division. Sci Rep. 2017 Aug 8;7(1):7627. doi: 10.1038/s41598-017-08213-5. PMID:28790446 doi:http://dx.doi.org/10.1038/s41598-017-08213-5
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