4l1c
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal structure of Dimerized N-terminal Domain of MinC== | |
| - | + | <StructureSection load='4l1c' size='340' side='right' caption='[[4l1c]], [[Resolution|resolution]] 2.28Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4l1c]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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 Escherichia coli UTI89])</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://www.rcsb.org/pdb/explore.do?structureId=4l1c RCSB], [http://www.ebi.ac.uk/pdbsum/4l1c PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Escherichia coli uti89]] | [[Category: Escherichia coli uti89]] | ||
| - | [[Category: An, J Y | + | [[Category: An, J Y]] |
| - | [[Category: Eom, S H | + | [[Category: Eom, S H]] |
| - | [[Category: Kang, G B | + | [[Category: Kang, G B]] |
| - | [[Category: Kang, J Y | + | [[Category: Kang, J Y]] |
| - | [[Category: Kim, T G | + | [[Category: Kim, T G]] |
| - | [[Category: Lee, J G | + | [[Category: Lee, J G]] |
| - | [[Category: Lee, Y | + | [[Category: Lee, Y]] |
| - | [[Category: Park, K R | + | [[Category: Park, K R]] |
| - | [[Category: Youn, H S | + | [[Category: Youn, H S]] |
[[Category: Antiparallel beta sheet]] | [[Category: Antiparallel beta sheet]] | ||
[[Category: Cell division inhibitor]] | [[Category: Cell division inhibitor]] | ||
Revision as of 14:53, 21 December 2014
Crystal structure of Dimerized N-terminal Domain of MinC
| |||||||||||
