5coj: Difference between revisions
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<StructureSection load='5coj' size='340' side='right'caption='[[5coj]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5coj' size='340' side='right'caption='[[5coj]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5coj]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5coj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5COJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5COJ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TZE:2-(4-METHYL-THIAZOL-5-YL)-ETHANOL'>TZE</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TZE:2-(4-METHYL-THIAZOL-5-YL)-ETHANOL'>TZE</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=5coj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5coj OCA], [https://pdbe.org/5coj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5coj RCSB], [https://www.ebi.ac.uk/pdbsum/5coj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5coj ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/THIM_STAAR THIM_STAAR] Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus]] | ||
[[Category: Betzel | [[Category: Betzel C]] | ||
[[Category: Cang | [[Category: Cang H]] | ||
[[Category: Drebes | [[Category: Drebes J]] | ||
[[Category: Eberle | [[Category: Eberle RJ]] | ||
[[Category: Kuenz | [[Category: Kuenz M]] | ||
[[Category: Oberthuer | [[Category: Oberthuer D]] | ||
[[Category: Wrenger | [[Category: Wrenger C]] | ||
Revision as of 15:20, 14 June 2023
Structure of Hydroxyethylthiazole kinase ThiM from Staphylococcus aureus in complex with native substrate 2-(4-methyl-1,3-thiazol-5-yl)ethanol.Structure of Hydroxyethylthiazole kinase ThiM from Staphylococcus aureus in complex with native substrate 2-(4-methyl-1,3-thiazol-5-yl)ethanol.
Structural highlights
FunctionTHIM_STAAR Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). Publication Abstract from PubMedInfections caused by the methicillin-resistant Staphylococcus aureus (MRSA) are today known to be a substantial threat for global health. Emerging multi-drug resistant bacteria have created a substantial need to identify and discover new drug targets and to develop novel strategies to treat bacterial infections. A promising and so far untapped antibiotic target is the biosynthesis of vitamin B1 (thiamin). Thiamin in its activated form, thiamin pyrophosphate, is an essential co-factor for all organisms. Therefore, thiamin analogous compounds, when introduced into the vitamin B1 biosynthetic pathway and further converted into non-functional co-factors by the bacterium can function as pro-drugs which thus block various co-factor dependent pathways. We characterized one of the key enzymes within the S. aureus vitamin B1 biosynthetic pathway, 5-(hydroxyethyl)-4-methylthiazole kinase (SaThiM; EC 2.7.1.50), a potential target for pro-drug compounds and analyzed the native structure of SaThiM and complexes with the natural substrate 5-(hydroxyethyl)-4-methylthiazole (THZ) and two selected substrate analogues. Structure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus - Insights into a novel pro-drug approach addressing MRSA infections.,Drebes J, Kunz M, Windshugel B, Kikhney AG, Muller IB, Eberle RJ, Oberthur D, Cang H, Svergun DI, Perbandt M, Betzel C, Wrenger C Sci Rep. 2016 Mar 10;6:22871. doi: 10.1038/srep22871. PMID:26960569[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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