6n14: Difference between revisions
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<StructureSection load='6n14' size='340' side='right'caption='[[6n14]], [[Resolution|resolution]] 1.52Å' scene=''> | <StructureSection load='6n14' size='340' side='right'caption='[[6n14]], [[Resolution|resolution]] 1.52Å' scene=''> | ||
== Structural highlights == | == 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 [ | <table><tr><td colspan='2'>[[6n14]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6N14 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5216947Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=6n14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n14 OCA], [https://pdbe.org/6n14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n14 RCSB], [https://www.ebi.ac.uk/pdbsum/6n14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n14 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/BLAC_MYCTU BLAC_MYCTU] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6n14" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6n14" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: | [[Category: Berkman CE]] | ||
[[Category: Choy CJ]] | |||
[[Category: Kang C]] | |||
[[Category: Moural TW]] | |||
[[Category: White DS]] | |||
Latest revision as of 09:43, 11 October 2023
Phosphoserine BlaC, Class A serine beta-lactamase from Mycobacterium tuberculosisPhosphoserine BlaC, Class A serine beta-lactamase from Mycobacterium tuberculosis
Structural highlights
FunctionPublication Abstract from PubMedMycobacterium 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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