4z7a: Difference between revisions
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''' | ==Structural and biochemical characterization of a non-functionally redundant M. tuberculosis (3,3) L,D-Transpeptidase, LdtMt5.== | ||
<StructureSection load='4z7a' size='340' side='right' caption='[[4z7a]], [[Resolution|resolution]] 1.98Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4z7a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z7A FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tur|3tur]], [[3u1q|3u1q]], [[3vae|3vae]], [[3u1p|3u1p]], [[3tx4|3tx4]]</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=4z7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z7a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4z7a RCSB], [http://www.ebi.ac.uk/pdbsum/4z7a PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
With multidrug-resistant cases of tuberculosis increasing globally, better antibiotic drugs and novel drug targets are becoming an urgent need. Traditional beta-lactam antibiotics that inhibit D,D-transpeptidases are not effective against mycobacteria, in part because mycobacteria rely mostly on L,D-transpeptidases for biosynthesis and maintenance of their peptidoglycan layer. This reliance plays a major role in drug resistance and persistence of Mycobacterium tuberculosis (Mtb) infections. The crystal structure at 1.7 A resolution of the Mtb L,D-transpeptidase Ldt(Mt2) containing a bound peptidoglycan fragment, reported here, provides information about catalytic site organization as well as substrate recognition by the enzyme. Based on our structural, kinetic, and calorimetric data, we propose a catalytic mechanism for Ldt(Mt2) in which both acyl-acceptor and acyl-donor substrates reach the catalytic site from the same, rather than different, entrances. Together, this information provides vital insights to facilitate development of drugs targeting this validated yet unexploited enzyme. | |||
Targeting the Cell Wall of Mycobacterium tuberculosis: Structure and Mechanism of L,D-Transpeptidase 2.,Erdemli SB, Gupta R, Bishai WR, Lamichhane G, Amzel LM, Bianchet MA Structure. 2012 Dec 5;20(12):2103-15. doi: 10.1016/j.str.2012.09.016. Epub 2012, Oct 25. PMID:23103390<ref>PMID:23103390</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Basta, L]] | ||
[[Category: Bianchet, M A]] | |||
[[Category: Ghosh, A]] | [[Category: Ghosh, A]] | ||
[[Category: Jakoncic, J]] | [[Category: Jakoncic, J]] | ||
[[Category: | [[Category: Lamichhane, G]] | ||
[[Category: Lloyd, E]] | |||
[[Category: Pan, Y]] | |||
[[Category: Townsend, G]] | [[Category: Townsend, G]] | ||
[[Category: Antibiotic]] | |||
[[Category: Carbapenem]] | |||
[[Category: Cell wall]] | |||
[[Category: Cell wall biosynthesis]] | |||
[[Category: Enzyme kinetic]] | |||
[[Category: Enzyme structure]] | |||
[[Category: Nitrocefin]] | |||
[[Category: Peptidoglycan]] | |||
[[Category: Transferase]] | |||
Revision as of 12:27, 2 September 2015
Structural and biochemical characterization of a non-functionally redundant M. tuberculosis (3,3) L,D-Transpeptidase, LdtMt5.
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