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| | ==The structure of the dimeric E.coli MinD-ATP complex== | | ==The structure of the dimeric E.coli MinD-ATP complex== |
| - | <StructureSection load='3q9l' size='340' side='right' caption='[[3q9l]], [[Resolution|resolution]] 2.34Å' scene=''> | + | <StructureSection load='3q9l' size='340' side='right'caption='[[3q9l]], [[Resolution|resolution]] 2.34Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3q9l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q9L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3q9l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q9L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">minD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">minD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [http://pdbe.org/3q9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [http://www.ebi.ac.uk/pdbsum/3q9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q9l 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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [https://pdbe.org/3q9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [https://www.ebi.ac.uk/pdbsum/3q9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q9l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI]] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the 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.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref> | + | [[https://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI]] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the 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.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Ecoli]] | | [[Category: Ecoli]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Holyoak, T]] | | [[Category: Holyoak, T]] |
| | [[Category: Lutkenhaus, J]] | | [[Category: Lutkenhaus, J]] |
| Structural highlights
Function
[MIND_ECOLI] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the 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.[1] [2]
Publication Abstract from PubMed
The three Min proteins spatially regulate Z ring positioning in Escherichia coli and are dynamically associated with the membrane. MinD binds to vesicles in the presence of ATP and can recruit MinC or MinE. Biochemical and genetic evidence indicate the binding sites for these two proteins on MinD overlap. Here we solved the structure of a hydrolytic-deficient mutant of MinD truncated for the C-terminal amphipathic helix involved in binding to the membrane. The structure solved in the presence of ATP is a dimer and reveals the face of MinD abutting the membrane. Using a combination of random and extensive site-directed mutagenesis additional residues important for MinE and MinC binding were identified. The location of these residues on the MinD structure confirms that the binding sites overlap and reveals that the binding sites are at the dimer interface and exposed to the cytosol. The location of the binding sites at the dimer interface offers a simple explanation for the ATP dependence of MinC and MinE binding to MinD.
Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.,Wu W, Park KT, Holyoak T, Lutkenhaus J Mol Microbiol. 2011 Jan 14. doi: 10.1111/j.1365-2958.2010.07536.x. PMID:21231967[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ de Boer PA, Crossley RE, Hand AR, Rothfield LI. The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site. EMBO J. 1991 Dec;10(13):4371-80. PMID:1836760
- ↑ 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
- ↑ Wu W, Park KT, Holyoak T, Lutkenhaus J. Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC. Mol Microbiol. 2011 Jan 14. doi: 10.1111/j.1365-2958.2010.07536.x. PMID:21231967 doi:10.1111/j.1365-2958.2010.07536.x
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