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==SOLUTION STRUCTURE OF THE MINE TOPOLOGICAL SPECIFICITY DOMAIN==
==SOLUTION STRUCTURE OF THE MINE TOPOLOGICAL SPECIFICITY DOMAIN==
<StructureSection load='1ev0' size='340' side='right'caption='[[1ev0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1ev0' size='340' side='right'caption='[[1ev0]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ev0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EV0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ev0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EV0 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=1ev0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ev0 OCA], [https://pdbe.org/1ev0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ev0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ev0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ev0 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ev0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ev0 OCA], [https://pdbe.org/1ev0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ev0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ev0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ev0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MINE_ECOLI MINE_ECOLI]] Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.<ref>PMID:22380631</ref>
[https://www.uniprot.org/uniprot/MINE_ECOLI MINE_ECOLI] Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.<ref>PMID:22380631</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ev0 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ev0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Correct positioning of the division septum in Escherichia coli depends on the coordinated action of the MinC, MinD and MinE proteins. Topological specificity is conferred on the MinCD division inhibitor by MinE, which counters MinCD activity only in the vicinity of the preferred midcell division site. Here we report the structure of the homodimeric topological specificity domain of Escherichia coli MinE and show that it forms a novel alphabeta sandwich. Structure-directed mutagenesis of conserved surface residues has enabled us to identify a spatially restricted site on the surface of the protein that is critical for the topological specificity function of MinE.
Structural basis for the topological specificity function of MinE.,King GF, Shih YL, Maciejewski MW, Bains NP, Pan B, Rowland SL, Mullen GP, Rothfield LI Nat Struct Biol. 2000 Nov;7(11):1013-7. PMID:11062554<ref>PMID:11062554</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ev0" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: King, G F]]
[[Category: King GF]]
[[Category: Maciejewski, M W]]
[[Category: Maciejewski MW]]
[[Category: Mullen, G P]]
[[Category: Mullen GP]]
[[Category: Pan, B]]
[[Category: Pan B]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[Category: Mincd]]
[[Category: Mine]]
[[Category: Minicell]]
[[Category: Topological specificity]]

Revision as of 13:06, 20 March 2024

SOLUTION STRUCTURE OF THE MINE TOPOLOGICAL SPECIFICITY DOMAINSOLUTION STRUCTURE OF THE MINE TOPOLOGICAL SPECIFICITY DOMAIN

Structural highlights

1ev0 is a 2 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MINE_ECOLI Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ 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
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