4gcl
From Proteopedia
(Difference between revisions)
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- | + | ==structure of no-dna factor== | |
- | ===structure | + | <StructureSection load='4gcl' size='340' side='right' caption='[[4gcl]], [[Resolution|resolution]] 2.65Å' scene=''> |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[4gcl]] is a 12 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=4GCL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GCL FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gck|4gck]], [[4gct|4gct]], [[4gcu|4gcu]], [[4gfk|4gfk]], [[4gfl|4gfl]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ttk, slmA, UTI89_C4185 ([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=4gcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gcl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gcl RCSB], [http://www.ebi.ac.uk/pdbsum/4gcl PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The spatial and temporal control of Filamenting temperature sensitive mutant Z (FtsZ) Z-ring formation is crucial for proper cell division in bacteria. In Escherichia coli, the synthetic lethal with a defective Min system (SlmA) protein helps mediate nucleoid occlusion, which prevents chromosome fragmentation by binding FtsZ and inhibiting Z-ring formation over the nucleoid. However, to perform its function, SlmA must be bound to the nucleoid. To deduce the basis for this chromosomal requirement, we performed biochemical, cellular, and structural studies. Strikingly, structures show that SlmA dramatically distorts DNA, allowing it to bind as an orientated dimer-of-dimers. Biochemical data indicate that SlmA dimer-of-dimers can spread along the DNA. Combined structural and biochemical data suggest that this DNA-activated SlmA oligomerization would prevent FtsZ protofilament propagation and bundling. Bioinformatic analyses localize SlmA DNA sites near membrane-tethered chromosomal regions, and cellular studies show that SlmA inhibits FtsZ reservoirs from forming membrane-tethered Z rings. Thus, our combined data indicate that SlmA DNA helps block Z-ring formation over chromosomal DNA by forming higher-order protein-nucleic acid complexes that disable FtsZ filaments from coalescing into proper structures needed for Z-ring creation. | ||
- | + | SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid.,Tonthat NK, Milam SL, Chinnam N, Whitfill T, Margolin W, Schumacher MA Proc Natl Acad Sci U S A. 2013 Jun 10. PMID:23754405<ref>PMID:23754405</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: Schumacher, M A | + | [[Category: Schumacher, M A]] |
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Dna binding protein-dna complex]] | [[Category: Dna binding protein-dna complex]] |
Revision as of 10:42, 21 December 2014
structure of no-dna factor
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