3bti

From Proteopedia

(Difference between revisions)

Revision as of 20:48, 5 August 2016

crystal structure of QacR(E58Q) bound to berberine

Structural highlights

3bti is a 4 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1jum, 3bt9, 3btc, 1jup, 1jty, 1rkw, 3btj
Gene:	qacR (Staphylococcus aureus)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[QACR_STAAM] 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 (By similarity).

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 PubMed

The Staphylococcus aureus multidrug binding protein QacR binds to a broad spectrum of structurally dissimilar cationic, lipophilic drugs. Our previous structural analyses suggested that five QacR glutamic acid residues are critical for charge neutralization and specification of certain drugs. For example, E57 and E58 interact with berberine and with one of the positively charged moieties of the bivalent drug dequalinium. Here we report the structural and biochemical effects of substituting E57 and E58 with alanine and glutamine. Unexpectedly, individual substitutions of these residues did not significantly affect QacR drug binding affinity. Structures of QacR(E57Q) and QacR(E58Q) bound to dequalinium indicated that E57 and E58 are redundant for charge neutralization. The most significant finding was that berberine was reoriented in the QacR multidrug binding pocket so that its positive charge was neutralized by side chain oxygen atoms and aromatic residues. Together, these data emphasize the remarkable versatility of the QacR multidrug binding pocket, illustrating that the capacity of QacR to bind myriad cationic drugs is largely governed by the presence in the pocket of a redundancy of polar, charged, and aromatic residues that are capable of electrostatic neutralization.

QacR-cation recognition is mediated by a redundancy of residues capable of charge neutralization.,Peters KM, Schuman JT, Skurray RA, Brown MH, Brennan RG, Schumacher MA Biochemistry. 2008 Aug 5;47(31):8122-9. Epub 2008 Jul 11. PMID:18616285^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Peters KM, Schuman JT, Skurray RA, Brown MH, Brennan RG, Schumacher MA. QacR-cation recognition is mediated by a redundancy of residues capable of charge neutralization. Biochemistry. 2008 Aug 5;47(31):8122-9. Epub 2008 Jul 11. PMID:18616285 doi:http://dx.doi.org/10.1021/bi8008246

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bti"

@@ Line 1: / Line 1: @@
 ==crystal structure of QacR(E58Q) bound to berberine==
 <StructureSection load='3bti' size='340' side='right' caption='[[3bti]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jum|1jum]], [[3bt9|3bt9]], [[3btc|3btc]], [[1jup|1jup]], [[1jty|1jty]], [[1rkw|1rkw]], [[3btj|3btj]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">qacR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])</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=3bti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bti OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bti RCSB], [http://www.ebi.ac.uk/pdbsum/3bti 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=3bti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bti OCA], [http://pdbe.org/3bti PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bti RCSB], [http://www.ebi.ac.uk/pdbsum/3bti PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bti ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bti ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3bti" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3bti

From Proteopedia

Revision as of 20:48, 5 August 2016

crystal structure of QacR(E58Q) bound to berberine

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox