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TitleStructure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus - Insights into a novel pro-drug approach addressing MRSA infections.
Journal, issue, pagesSci Rep, Vol. 6, Page 22871, Year 2016
Publish dateMar 10, 2016
AuthorsJulia Drebes / Madeleine Künz / Björn Windshügel / Alexey G Kikhney / Ingrid B Müller / Raphael J Eberle / Dominik Oberthür / Huaixing Cang / Dmitri I Svergun / Markus Perbandt / Christian Betzel / Carsten Wrenger /
PubMed AbstractInfections 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 ...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.
External linksSci Rep / PubMed:26960569 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution1.62 - 2.09 Å
Structure data

SASDAX8:
Ribokinase ThiM (ThiM)
Method: SAXS/SANS

PDB-5cga:
Structure of Hydroxyethylthiazole kinase ThiM from Staphylococcus aureus in complex with substrate analog 2-(1,3,5-trimethyl-1H-pyrazole-4-yl)ethanol
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

PDB-5cge:
Structure of Hydroxyethylthiazole Kinase ThiM from Staphylococcus aureus in complex with substrate analog 2-(2-methyl-1H-imidazole-1-yl)ethanol
Method: X-RAY DIFFRACTION / Resolution: 1.62 Å

PDB-5cm5:
Structure of Hydroxyethylthiazole Kinase ThiM from Staphylococcus aureus
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

PDB-5coj:
Structure of Hydroxyethylthiazole kinase ThiM from Staphylococcus aureus in complex with native substrate 2-(4-methyl-1,3-thiazol-5-yl)ethanol.
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-KP6:
2-(1,3,5-trimethyl-1H-pyrazol-4-yl)ethanol

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-51F:
2-(2-methyl-1H-imidazol-1-yl)ethanol

ChemComp-TZE:
2-(4-METHYL-THIAZOL-5-YL)-ETHANOL

Source
  • staphylococcus aureus (bacteria)
  • staphylococcus aureus mrsa252 (bacteria)
  • staphylococcus aureus subsp. aureus mrsa252 (bacteria)
KeywordsTRANSFERASE / Bacterial Thiamine Biosynthesis / Hydroxyethylthiazole Kinase / Substrate Analog / 2-(4-methyl-1 / 3-thiazol-5-yl)ethanol

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