5w8p

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<StructureSection load='5w8p' size='340' side='right'caption='[[5w8p]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
<StructureSection load='5w8p' size='340' side='right'caption='[[5w8p]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5w8p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myca9 Myca9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W8P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5w8p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacteroides_abscessus_ATCC_19977 Mycobacteroides abscessus ATCC 19977]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W8P FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">metX, MAB_3688 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=561007 MYCA9])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5w8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w8p OCA], [https://pdbe.org/5w8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w8p RCSB], [https://www.ebi.ac.uk/pdbsum/5w8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w8p ProSAT]</span></td></tr>
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<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=5w8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w8p OCA], [http://pdbe.org/5w8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w8p RCSB], [http://www.ebi.ac.uk/pdbsum/5w8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w8p ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/B1MG17_MYCA9 B1MG17_MYCA9]] Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.[HAMAP-Rule:MF_00296]
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[https://www.uniprot.org/uniprot/B1MG17_MYCA9 B1MG17_MYCA9] Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.[HAMAP-Rule:MF_00296]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5w8p" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homoserine O-acetyltransferase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myca9]]
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[[Category: Mycobacteroides abscessus ATCC 19977]]
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[[Category: Korotkov, K V]]
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[[Category: Korotkov KV]]
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[[Category: Reed, R W]]
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[[Category: Reed RW]]
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[[Category: Rodriguez, E S]]
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[[Category: Rodriguez ES]]
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[[Category: Homoserine o-acetyltransferase]]
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[[Category: Homoserine o-trans-acetylase]]
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[[Category: Hta]]
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[[Category: Methionine biosynthesis]]
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[[Category: Metx]]
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[[Category: Rv3341]]
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[[Category: Transferase]]
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Current revision

Homoserine transacetylase MetX from Mycobacterium abscessus

PDB ID 5w8p

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