5CM5: Structure Of Hydroxyethylthiazole Kinase Thim From Staphylococcus Aureus

Citation:
Abstract
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.
PDB ID: 5CM5Download
MMDB ID: 137671
PDB Deposition Date: 2015/7/16
Updated in MMDB: 2016/03
Experimental Method:
x-ray diffraction
Resolution: 2.09  Å
Source Organism:
Similar Structures:
Biological Unit for 5CM5: trimeric; determined by author and by software (PISA)
Molecular Components in 5CM5
Label Count Molecule
Proteins (3 molecules)
3
Hydroxyethylthiazole Kinase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.