View source for 5cge


==Structure of Hydroxyethylthiazole Kinase ThiM from Staphylococcus aureus in complex with substrate analog 2-(2-methyl-1H-imidazole-1-yl)ethanol==
<StructureSection load='5cge' size='340' side='right'caption='[[5cge]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cge]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MRSA252 Staphylococcus aureus subsp. aureus MRSA252]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CGE 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]] 1.62&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=51F:2-(2-METHYL-1H-IMIDAZOL-1-YL)ETHANOL'>51F</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5cge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cge OCA], [https://pdbe.org/5cge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cge RCSB], [https://www.ebi.ac.uk/pdbsum/5cge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cge ProSAT]</span></td></tr>
</table>
== 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;">
== Publication Abstract from PubMed ==
Infections 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<ref>PMID:26960569</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cge" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus MRSA252]]
[[Category: Betzel C]]
[[Category: Cang H]]
[[Category: Drebes J]]
[[Category: Kuenz M]]
[[Category: Windshuegel B]]
[[Category: Wrenger C]]