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3p2f

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Current revision (11:20, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3p2f' size='340' side='right'caption='[[3p2f]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3p2f' size='340' side='right'caption='[[3p2f]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3p2f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33617 Atcc 33617]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P2F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3p2f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P2F FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3p2h|3p2h]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tofI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=337 ATCC 33617])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3p2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p2f OCA], [https://pdbe.org/3p2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p2f RCSB], [https://www.ebi.ac.uk/pdbsum/3p2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p2f 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=3p2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p2f OCA], [https://pdbe.org/3p2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p2f RCSB], [https://www.ebi.ac.uk/pdbsum/3p2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p2f ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q4VSJ8_BURGB Q4VSJ8_BURGB]
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Quorum sensing (QS) controls certain behaviors of bacteria in response to population density. In Gram-negative bacteria, QS is often mediated by N-acyl-l-homoserine lactones (acyl-HSLs). Because QS influences the virulence of many pathogenic bacteria, synthetic inhibitors of acyl-HSL synthases might be useful therapeutically for controlling pathogens. However, rational design of a potent QS antagonist has been thwarted by the lack of information concerning the binding interactions between acyl-HSL synthases and their ligands. In the Gram-negative bacterium Burkholderia glumae, QS controls virulence, motility, and protein secretion and is mediated by the binding of N-octanoyl-l-HSL (C8-HSL) to its cognate receptor, TofR. C8-HSL is synthesized by the acyl-HSL synthase TofI. In this study, we characterized two previously unknown QS inhibitors identified in a focused library of acyl-HSL analogs. Our functional and X-ray crystal structure analyses show that the first inhibitor, J8-C8, binds to TofI, occupying the binding site for the acyl chain of the TofI cognate substrate, acylated acyl-carrier protein. Moreover, the reaction byproduct, 5'-methylthioadenosine, independently binds to the binding site for a second substrate, S-adenosyl-l-methionine. Closer inspection of the mode of J8-C8 binding to TofI provides a likely molecular basis for the various substrate specificities of acyl-HSL synthases. The second inhibitor, E9C-3oxoC6, competitively inhibits C8-HSL binding to TofR. Our analysis of the binding of an inhibitor and a reaction byproduct to an acyl-HSL synthase may facilitate the design of a new class of QS-inhibiting therapeutic agents.
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Small-molecule inhibitor binding to an N-acyl-homoserine lactone synthase.,Chung J, Goo E, Yu S, Choi O, Lee J, Kim J, Kim H, Igarashi J, Suga H, Moon JS, Hwang I, Rhee S Proc Natl Acad Sci U S A. 2011 Jul 19;108(29):12089-94. Epub 2011 Jul 5. PMID:21730159<ref>PMID:21730159</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3p2f" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 33617]]
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[[Category: Burkholderia glumae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Rhee, S]]
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[[Category: Rhee S]]
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[[Category: Yu, S]]
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[[Category: Yu S]]
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[[Category: Acyl-acp binding]]
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[[Category: Sam binding]]
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[[Category: Signaling protein]]
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[[Category: Synthase]]
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Current revision

Crystal structure of TofI in an apo form

PDB ID 3p2f

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