3q7z: Difference between revisions
New page: '''Unreleased structure''' The entry 3q7z is ON HOLD Authors: Borbulevych, O.Y., Mobashery, S, Baker, B.M. Description: CBAP-acylated BlaR1 sensor domain from Staphylococcus aureus |
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The | ==CBAP-acylated BlaR1 sensor domain from Staphylococcus aureus== | ||
<StructureSection load='3q7z' size='340' side='right'caption='[[3q7z]], [[Resolution|resolution]] 1.87Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3q7z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q7Z FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOU:(2R,4S)-2-[(1R)-1-{[(2-CARBOXYBIPHENYL-2-YL)CARBONYL]AMINO}-2-OXOETHYL]-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>BOU</scene></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=3q7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q7z OCA], [https://pdbe.org/3q7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q7z RCSB], [https://www.ebi.ac.uk/pdbsum/3q7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q7z ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7WU28_STAAU Q7WU28_STAAU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The integral membrane protein BlaR1 of methicillin-resistant Staphylococcus aureus senses the presence of beta-lactam antibiotics in the milieu and transduces the information to the cytoplasm, where the biochemical events that unleash induction of antibiotic resistance mechanisms take place. We report herein by two-dimensional and three-dimensional NMR experiments of the sensor domain of BlaR1 in solution and by determination of an x-ray structure for the apo protein that Lys-392 of the antibiotic-binding site is posttranslationally modified by N(zeta)-carboxylation. Additional crystallographic and NMR data reveal that on acylation of Ser-389 by antibiotics, Lys-392 experiences N(zeta)-decarboxylation. This unique process, termed the lysine N(zeta)-decarboxylation switch, arrests the sensor domain in the activated ("on") state, necessary for signal transduction and all the subsequent biochemical processes. We present structural information on how this receptor activation process takes place, imparting longevity to the antibiotic-receptor complex that is needed for the induction of the antibiotic-resistant phenotype in methicillin-resistant S. aureus. | |||
Lysine Nzeta-decarboxylation switch and activation of the beta-lactam sensor domain of BlaR1 protein of methicillin-resistant Staphylococcus aureus.,Borbulevych O, Kumarasiri M, Wilson B, Llarrull LI, Lee M, Hesek D, Shi Q, Peng J, Baker BM, Mobashery S J Biol Chem. 2011 Sep 9;286(36):31466-72. Epub 2011 Jul 20. PMID:21775440<ref>PMID:21775440</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3q7z" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus]] | |||
[[Category: Baker BM]] | |||
[[Category: Borbulevych OY]] | |||
[[Category: Mobashery S]] | |||
Latest revision as of 09:06, 17 October 2024
CBAP-acylated BlaR1 sensor domain from Staphylococcus aureusCBAP-acylated BlaR1 sensor domain from Staphylococcus aureus
Structural highlights
FunctionPublication Abstract from PubMedThe integral membrane protein BlaR1 of methicillin-resistant Staphylococcus aureus senses the presence of beta-lactam antibiotics in the milieu and transduces the information to the cytoplasm, where the biochemical events that unleash induction of antibiotic resistance mechanisms take place. We report herein by two-dimensional and three-dimensional NMR experiments of the sensor domain of BlaR1 in solution and by determination of an x-ray structure for the apo protein that Lys-392 of the antibiotic-binding site is posttranslationally modified by N(zeta)-carboxylation. Additional crystallographic and NMR data reveal that on acylation of Ser-389 by antibiotics, Lys-392 experiences N(zeta)-decarboxylation. This unique process, termed the lysine N(zeta)-decarboxylation switch, arrests the sensor domain in the activated ("on") state, necessary for signal transduction and all the subsequent biochemical processes. We present structural information on how this receptor activation process takes place, imparting longevity to the antibiotic-receptor complex that is needed for the induction of the antibiotic-resistant phenotype in methicillin-resistant S. aureus. Lysine Nzeta-decarboxylation switch and activation of the beta-lactam sensor domain of BlaR1 protein of methicillin-resistant Staphylococcus aureus.,Borbulevych O, Kumarasiri M, Wilson B, Llarrull LI, Lee M, Hesek D, Shi Q, Peng J, Baker BM, Mobashery S J Biol Chem. 2011 Sep 9;286(36):31466-72. Epub 2011 Jul 20. PMID:21775440[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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