View source for 6pux


==Homoserine transacetylase MetX from Mycobacterium tuberculosis==
<StructureSection load='6pux' size='340' side='right'caption='[[6pux]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pux]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PUX 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6pux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pux OCA], [https://pdbe.org/6pux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pux RCSB], [https://www.ebi.ac.uk/pdbsum/6pux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pux ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/METXA_MYCTU METXA_MYCTU] Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mycobacterium tuberculosis is the cause of the world's most deadly infectious disease. Efforts are underway to target the methionine biosynthesis pathway, as it is not part of the host metabolism. The homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of this pathway. In order to facilitate structure-based drug design, we determined the high-resolution crystal structures of three MetX proteins, including M. tuberculosis (MtMetX), Mycolicibacterium abscessus (MaMetX), and Mycolicibacterium hassiacum (MhMetX). A comparison of homoserine transacetylases from other bacterial and fungal species reveals a high degree of structural conservation amongst the enzymes. Utilizing homologous structures with bound cofactors, we analyzed the potential ligandability of MetX. The deep active-site tunnel surrounding the catalytic serine yielded many consensus clusters during mapping, suggesting that MtMetX is highly druggable.

Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site.,Chaton CT, Rodriguez ES, Reed RW, Li J, Kenner CW, Korotkov KV Sci Rep. 2019 Dec 30;9(1):20267. doi: 10.1038/s41598-019-56722-2. PMID:31889085<ref>PMID:31889085</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pux" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Chaton CT]]
[[Category: Korotkov KV]]