4l1c
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28Å</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 == | ||
[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] | [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®/PubMed®, 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> | ||
Current revision
Crystal structure of Dimerized N-terminal Domain of MinC
| |||||||||||
Categories: Escherichia coli UTI89 | Large Structures | An JY | Eom SH | Kang GB | Kang JY | Kim TG | Lee JG | Lee Y | Park KR | Youn HS
