1xkz

<StructureSection load='1xkz' size='340' side='right' caption='[[1xkz]], [[Resolution|resolution]] 1.75&Aring;' scene=''>

<table><tr><td colspan='2'>[[1xkz]] is a 4 chain structure with sequence from [http://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=1XKZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XKZ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAZ:ACYLATED+CEFTAZIDIME'>CAZ</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1xkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xkz OCA], [http://pdbe.org/1xkz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xkz RCSB], [http://www.ebi.ac.uk/pdbsum/1xkz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xkz ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/BLAR_STAAU BLAR_STAAU]] BlaR1 is a potential penicillin-binding protein required for induction of beta-lactamase.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Methicillin-resistant strains of Staphylococcus aureus (MRSA) are the major cause of infections worldwide. Transcription of the beta-lactamase and PBP2a resistance genes is mediated by two closely related signal-transducing integral membrane proteins, BlaR1 and MecR1, upon binding of the beta-lactam inducer to the sensor domain. Herein we report the crystal structure at 1.75 A resolution of the sensor domain of BlaR1 in complex with a cephalosporin antibiotic. Activation of the signal transducer involves acylation of serine 389 by the beta-lactam antibiotic, a process promoted by the N-carboxylated side chain of Lys392. We present evidence that, on acylation, the lysine side chain experiences a spontaneous decarboxylation that entraps the sensor in its activated state. Kinetic determinations and quantum mechanical/molecular mechanical calculations and the interaction networks in the crystal structure shed light on how this unprecedented process for activation of a receptor may be achieved and provide insights into the mechanistic features that differentiate the signal-transducing receptor from the structurally related class D beta-lactamases, enzymes of antibiotic resistance.

X-ray crystal structure of the acylated beta-lactam sensor domain of BlaR1 from Staphylococcus aureus and the mechanism of receptor activation for signal transduction.,Birck C, Cha JY, Cross J, Schulze-Briese C, Meroueh SO, Schlegel HB, Mobashery S, Samama JP J Am Chem Soc. 2004 Nov 3;126(43):13945-7. PMID:15506754<ref>PMID:15506754</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1xkz" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Birck, C]]

[[Category: Cha, J Y]]

[[Category: Cross, J]]

[[Category: Meroueh, S O]]

[[Category: Mobashery, S]]

[[Category: Samama, J P]]

[[Category: Schlegel, H B]]

[[Category: Schulze-Briese, C]]

[[Category: Signaling protein]]