View source for 5xdm


==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]] 3.00&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.004&#8491;</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>
== Function ==
[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;">
== 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<ref>PMID:28790446</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xdm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Shen Q]]
[[Category: Yang S]]
[[Category: Zheng J]]