1s1s: Difference between revisions
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<StructureSection load='1s1s' size='340' side='right' caption='[[1s1s]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1s1s' size='340' side='right' caption='[[1s1s]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1s1s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1s1s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S1S FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=WAC:N-{3-[(12BS)-7-OXO-1,3,4,6,7,12B-HEXAHYDROINDOLO[2,3-A]QUINOLIZIN-12(2H)-YL]PROPYL}PROPANE-2-SULFONAMIDE'>WAC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=WAC:N-{3-[(12BS)-7-OXO-1,3,4,6,7,12B-HEXAHYDROINDOLO[2,3-A]QUINOLIZIN-12(2H)-YL]PROPYL}PROPANE-2-SULFONAMIDE'>WAC</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1s1j|1s1j]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1s1j|1s1j]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZIPA, B2412 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZIPA, B2412 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1s1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s1s RCSB], [http://www.ebi.ac.uk/pdbsum/1s1s PDBsum]</span></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=1s1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1s OCA], [http://pdbe.org/1s1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s1s RCSB], [http://www.ebi.ac.uk/pdbsum/1s1s PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1s1s" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Ding, W]] | [[Category: Ding, W]] | ||
[[Category: Dushin, E G]] | [[Category: Dushin, E G]] |
Revision as of 10:19, 11 September 2015
Crystal Structure of ZipA in complex with indoloquinolizin 10bCrystal Structure of ZipA in complex with indoloquinolizin 10b
Structural highlights
Function[ZIPA_ECOLI] Interacts directly with the cell division protein FtsZ. Probable receptor for the septal ring structure, may anchor it to the inner-membrane.[HAMAP-Rule:MF_00509] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe binding of FtsZ to ZipA is a potential target for antibacterial therapy. Based on a small molecule inhibitor of the ZipA-FtsZ interaction, a parallel synthesis of small molecules was initiated which targeted a key region of ZipA involved in FtsZ binding. The X-ray crystal structure of one of these molecules complexed with ZipA was solved. The structure revealed an unexpected binding mode, facilitated by desolvation of a loosely bound surface water. Design and synthesis of indolo[2,3-a]quinolizin-7-one inhibitors of the ZipA-FtsZ interaction.,Jennings LD, Foreman KW, Rush TS 3rd, Tsao DH, Mosyak L, Li Y, Sukhdeo MN, Ding W, Dushin EG, Kenny CH, Moghazeh SL, Petersen PJ, Ruzin AV, Tuckman M, Sutherland AG Bioorg Med Chem Lett. 2004 Mar 22;14(6):1427-31. PMID:15006376[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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