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==Crystal structure of Dimerized N-terminal Domain of MinC==
==Crystal structure of Dimerized N-terminal Domain of MinC==
<StructureSection load='4l1c' size='340' side='right' caption='[[4l1c]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
<StructureSection load='4l1c' size='340' side='right'caption='[[4l1c]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4l1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecout Ecout]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L1C FirstGlance]. <br>
<table><tr><td colspan='2'>[[4l1c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UTI89 Escherichia coli UTI89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L1C FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECDH1ME8569_1115, EcDH1_2472, minC, UTI89_C1361 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 ECOUT])</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]] 2.28&#8491;</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=4l1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l1c OCA], [http://pdbe.org/4l1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l1c RCSB], [http://www.ebi.ac.uk/pdbsum/4l1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l1c 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=4l1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l1c OCA], [https://pdbe.org/4l1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l1c RCSB], [https://www.ebi.ac.uk/pdbsum/4l1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l1c ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q1RCS1_ECOUT Q1RCS1_ECOUT]] 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 (By similarity).[HAMAP-Rule:MF_00267][SAAS:SAAS013033_004_034544]  
[https://www.uniprot.org/uniprot/Q1RCS1_ECOUT Q1RCS1_ECOUT] 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 (By similarity).[HAMAP-Rule:MF_00267][SAAS:SAAS013033_004_034544]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proper cell division at the mid-site of gram-negative bacteria reflects critical regulation by the min system (MinC, MinD and MinE) of the cytokinetic Z ring, which is a polymer composed of FtsZ subunits. MinC and MinD act together to inhibit aberrantly positioned Z-ring formation. MinC consists of two domains: an N-terminal domain (MinCNTD), which interacts with FtsZ and inhibits FtsZ polymerization, and a C-terminal domain (MinCCTD), which interacts with MinD and inhibits the bundling of FtsZ filaments. These two domains reportedly function together, and both are essential for normal cell division. The full-length dimeric structure of MinC from Thermotoga maritima has been reported, and shows that MinC dimerization occurs via MinCCTD; MinCNTD is not involved in dimerization. Here the crystal structure of Escherichia coli MinCNTD (EcoMinCNTD) is reported. EcoMinCNTD forms a dimer via domain swapping between the first beta strands in each subunit. It is therefore suggested that the dimerization of full-length EcoMinC occurs via both MinCCTD and MinCNTD, and that the dimerized EcoMinCNTD likely plays an important role in inhibiting aberrant Z-ring localization.
 
Crystal structure of the N-terminal domain of MinC dimerized via domain swapping.,An JY, Kim TG, Park KR, Lee JG, Youn HS, Lee Y, Kang JY, Kang GB, Eom SH J Synchrotron Radiat. 2013 Nov;20(Pt 6):984-8. doi: 10.1107/S0909049513022760., Epub 2013 Oct 2. PMID:24121353<ref>PMID:24121353</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4l1c" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecout]]
[[Category: Escherichia coli UTI89]]
[[Category: An, J Y]]
[[Category: Large Structures]]
[[Category: Eom, S H]]
[[Category: An JY]]
[[Category: Kang, G B]]
[[Category: Eom SH]]
[[Category: Kang, J Y]]
[[Category: Kang GB]]
[[Category: Kim, T G]]
[[Category: Kang JY]]
[[Category: Lee, J G]]
[[Category: Kim TG]]
[[Category: Lee, Y]]
[[Category: Lee JG]]
[[Category: Park, K R]]
[[Category: Lee Y]]
[[Category: Youn, H S]]
[[Category: Park KR]]
[[Category: Antiparallel beta sheet]]
[[Category: Youn HS]]
[[Category: Cell division inhibitor]]
[[Category: Ftsz]]
[[Category: Protein binding]]
[[Category: Swapping]]
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