View source for 6n14


==Phosphoserine BlaC, Class A serine beta-lactamase from Mycobacterium tuberculosis==
<StructureSection load='6n14' size='340' side='right'caption='[[6n14]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6n14]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N14 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N14 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=6n14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n14 OCA], [http://pdbe.org/6n14 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n14 RCSB], [http://www.ebi.ac.uk/pdbsum/6n14 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n14 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mycobacterium tuberculosis, the pathogen responsible for tuberculosis (TB), is the leading cause of death from infectious disease worldwide. The class A serine beta-lactamase BlaC confers Mycobacterium tuberculosis resistance to conventional beta-lactam antibiotics. As the primary mechanism of bacterial resistance to beta-lactam antibiotics, the expression of a beta-lactamase by Mycobacterium tuberculosis results in hydrolysis of the beta-lactam ring and deactivation of these antibiotics. In this study, we conducted protein X-ray crystallographic analysis of the inactivation of BlaC, upon exposure to the inhibitor bis(benzoyl) phosphate. Crystal structure data confirms that serine beta-lactamase is phosphorylated at the catalytic serine residue (Ser-70) by this phosphate-based inactivator. This new crystallographic evidence suggests a mechanism for phosphorylation of BlaC inhibition by bis(benzoyl) phosphate over acylation. Additionally, we confirmed that bis(benzoyl) phosphate inactivated BlaC in a time-dependent manner.

Crystal Structure of Phosphoserine BlaC from Mycobacterium tuberculosis Inactivated by Bis(Benzoyl) Phosphate.,Moural TW, White DS, Choy CJ, Kang C, Berkman CE Int J Mol Sci. 2019 Jul 2;20(13). pii: ijms20133247. doi: 10.3390/ijms20133247. PMID:31269656<ref>PMID:31269656</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6n14" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Berkman, C E]]
[[Category: Choy, C J]]
[[Category: Kang, C]]
[[Category: Moural, T W]]
[[Category: White, D S]]
[[Category: Hydrolase]]
[[Category: Inhibitor]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Phosphoserine]]