1jum: Difference between revisions
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<StructureSection load='1jum' size='340' side='right'caption='[[1jum]], [[Resolution|resolution]] 2.98Å' scene=''> | <StructureSection load='1jum' size='340' side='right'caption='[[1jum]], [[Resolution|resolution]] 2.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jum]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1jum]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JUM FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BER:BERBERINE'>BER</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BER:BERBERINE'>BER</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jt0|1jt0]], [[1jt6|1jt6]], [[1jtx|1jtx]], [[1jty|1jty]], [[1jup|1jup]], [[1jus|1jus]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jt0|1jt0]], [[1jt6|1jt6]], [[1jtx|1jtx]], [[1jty|1jty]], [[1jup|1jup]], [[1jus|1jus]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jum OCA], [https://pdbe.org/1jum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jum RCSB], [https://www.ebi.ac.uk/pdbsum/1jum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jum ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/QACR_STAAU QACR_STAAU]] Transcriptional repressor of qacA. Binds to IR1, an unusually long 28 bp operator, which is located downstream from the qacA promoter and overlaps its transcription start site. QacR is induced from its IR1 site by binding to one of many structurally dissimilar cationic lipophilic compounds, which are also substrates of QacA. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 17:35, 27 October 2021
Crystal structure of the multidrug binding transcriptional repressor QacR bound to the natural drug berberineCrystal structure of the multidrug binding transcriptional repressor QacR bound to the natural drug berberine
Structural highlights
Function[QACR_STAAU] Transcriptional repressor of qacA. Binds to IR1, an unusually long 28 bp operator, which is located downstream from the qacA promoter and overlaps its transcription start site. QacR is induced from its IR1 site by binding to one of many structurally dissimilar cationic lipophilic compounds, which are also substrates of QacA. 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 Staphylococcus aureus multidrug binding protein QacR represses transcription of the qacA multidrug transporter gene and is induced by structurally diverse cationic lipophilic drugs. Here, we report the crystal structures of six QacR-drug complexes. Compared to the DNA bound structure, drug binding elicits a coil-to-helix transition that causes induction and creates an expansive multidrug-binding pocket, containing four glutamates and multiple aromatic and polar residues. These structures indicate the presence of separate but linked drug-binding sites within a single protein. This multisite drug-binding mechanism is consonant with studies on multidrug resistance transporters. Structural mechanisms of QacR induction and multidrug recognition.,Schumacher MA, Miller MC, Grkovic S, Brown MH, Skurray RA, Brennan RG Science. 2001 Dec 7;294(5549):2158-63. PMID:11739955[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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