5w8o
From Proteopedia
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(New page: ==Homoserine transacetylase MetA from Mycobacterium hassiacum== <StructureSection load='5w8o' size='340' side='right' caption='5w8o, resolution 1.47Å' scene=''> =...) |
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| - | ==Homoserine transacetylase | + | ==Homoserine transacetylase MetX from Mycobacterium hassiacum== |
| - | <StructureSection load='5w8o' size='340' side='right' caption='[[5w8o]], [[Resolution|resolution]] 1.47Å' scene=''> | + | <StructureSection load='5w8o' size='340' side='right'caption='[[5w8o]], [[Resolution|resolution]] 1.47Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5w8o]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W8O OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5w8o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_hassiacum_DSM_44199 Mycolicibacterium hassiacum DSM 44199]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W8O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.47Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5w8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w8o OCA], [https://pdbe.org/5w8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w8o RCSB], [https://www.ebi.ac.uk/pdbsum/5w8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w8o ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/K5B926_MYCHD K5B926_MYCHD] Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.[HAMAP-Rule:MF_00296] |
| + | <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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5w8o" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mycolicibacterium hassiacum DSM 44199]] |
| - | [[Category: | + | [[Category: Korotkov KV]] |
| - | [[Category: | + | [[Category: Li J]] |
| - | [[Category: | + | [[Category: Reed RW]] |
| - | [[Category: | + | [[Category: Rodriguez ES]] |
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Current revision
Homoserine transacetylase MetX from Mycobacterium hassiacum
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