6rlg: Difference between revisions

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'''Unreleased structure'''


The entry 6rlg is ON HOLD until Paper Publication
==Crystal structure of LdtMt2 from Mycobacterium tuberculosis==
<StructureSection load='6rlg' size='340' side='right'caption='[[6rlg]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rlg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RLG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RLG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=6rlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlg OCA], [http://pdbe.org/6rlg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rlg RCSB], [http://www.ebi.ac.uk/pdbsum/6rlg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlg ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/LDT2_MYCTO LDT2_MYCTO]] Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems. Is essential for virulence in a mouse model of acute infection.<ref>PMID:20305661</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The l,d-transpeptidases (Ldts) are promising antibiotic targets for treating tuberculosis. We report screening of cysteine-reactive inhibitors against LdtMt2 from Mycobacterium tuberculosis. Structural studies on LdtMt2 with potent inhibitor ebselen reveal opening of the benzisoselenazolone ring by a nucleophilic cysteine, forming a complex involving extensive hydrophobic interactions with a substrate-binding loop.


Authors:  
Targeting the Mycobacterium tuberculosis transpeptidase LdtMt2 with cysteine-reactive inhibitors including ebselen.,de Munnik M, Lohans CT, Lang PA, Langley GW, Malla TR, Tumber A, Schofield CJ, Brem J Chem Commun (Camb). 2019 Aug 5. doi: 10.1039/c9cc04145a. PMID:31380528<ref>PMID:31380528</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6rlg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Brem, J]]
[[Category: Lohans, C]]
[[Category: Schofield, C]]
[[Category: Antibiotic resistance]]
[[Category: Antimicrobial protein]]
[[Category: Beta lactmase]]
[[Category: Tuberculosis]]
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