View source for 7bva


==Crystal structure of UDP-N-acetylmuramic Acid L-alanine ligase (MurC) from Mycobacterium bovis==
<StructureSection load='7bva' size='340' side='right'caption='[[7bva]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7bva]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_variant_bovis_AF2122/97 Mycobacterium tuberculosis variant bovis AF2122/97]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BVA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.303&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7bva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bva OCA], [https://pdbe.org/7bva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bva RCSB], [https://www.ebi.ac.uk/pdbsum/7bva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bva ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MURC_MYCBO MURC_MYCBO] Cell wall formation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidoglycan comprises repeating units of N-acetylmuramic acid, N-acetylglucosamine and short cross-linking peptides. After the conversion of UDP-N-acetylglucosamine (UNAG) to UDP-N-acetylmuramic acid (UNAM) by the MurA and MurB enzymes, an amino acid is added to UNAM by UDP-N-acetylmuramic acid L-alanine ligase (MurC). As peptidoglycan is an essential component of the bacterial cell wall, the enzymes involved in its biosynthesis represent promising targets for the development of novel antibacterial drugs. Here, the crystal structure of Mycobacterium bovis MurC (MbMurC) is reported, which exhibits a three-domain architecture for the binding of UNAM, ATP and an amino acid as substrates, with a nickel ion at the domain interface. The ATP-binding loop adopts a conformation that is not seen in other MurCs. In the UNAG-bound structure of MbMurC, the substrate mimic interacts with the UDP-binding domain of MbMurC, which does not invoke rearrangement of the three domains. Interestingly, the glycine-rich loop of the UDP-binding domain of MbMurC interacts through hydrogen bonds with the glucose moiety of the ligand, but not with the pyrophosphate moiety. These findings suggest that UNAG analogs might serve as potential candidates for neutralizing the catalytic activity of bacterial MurC.

Crystal structures of UDP-N-acetylmuramic acid L-alanine ligase (MurC) from Mycobacterium bovis with and without UDP-N-acetylglucosamine.,Seo PW, Park SY, Hofmann A, Kim JS Acta Crystallogr D Struct Biol. 2021 May 1;77(Pt 5):618-627. doi:, 10.1107/S2059798321002199. Epub 2021 Apr 14. PMID:33950018<ref>PMID:33950018</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7bva" style="background-color:#fffaf0;"></div>

==See Also==
*[[Enoylpyruvate transferase 3D structures|Enoylpyruvate transferase 3D structures]]
*[[Mur ligase|Mur ligase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis variant bovis AF2122/97]]
[[Category: Kim JS]]
[[Category: Seo PW]]