5VYQ

Crystal structure of the N-formyltransferase Rv3404c from mycobacterium tuberculosis in complex with YDP-Qui4N and folinic acid

Summary for 5VYQ

• Entry DOI: 10.2210/pdb5vyq/pdb
• Related: 5VYR 5VYS 5VYT 5VYU
• Descriptor: Uncharacterized protein, POTASSIUM ION, N-{[4-({[(6R)-2-amino-5-formyl-4-oxo-1,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)phenyl]carbonyl}-L-glutamic acid, ... (11 entities in total)
• Functional Keywords: formyltransferase, deoxysugar, transferase
• Biological source: Mycobacterium tuberculosis CAS/NITR204
• Total number of polymer chains: 2
• Total formula weight: 60487.76

Authors

Dunsirn, M.M.,Thoden, J.B.,Holden, H.M. (deposition date: 2017-05-26, release date: 2017-07-12, Last modification date: 2023-10-04)

Primary citation

Dunsirn, M.M.,Thoden, J.B.,Gilbert, M.,Holden, H.M.
Biochemical Investigation of Rv3404c from Mycobacterium tuberculosis.
Biochemistry, 56:3818-3825, 2017

PubMed Abstract: The causative agent of tuberculosis, Mycobacterium tuberculosis, is a bacterium with a complex cell wall and a complicated life cycle. The genome of M. tuberculosis contains well over 4000 genes thought to encode proteins. One of these codes for a putative enzyme referred to as Rv3404c, which has attracted research attention as a potential virulence factor for over 12 years. Here we demonstrate that Rv3404c functions as a sugar N-formyltransferase that converts dTDP-4-amino-4,6-dideoxyglucose into dTDP-4-formamido-4,6-dideoxyglucose using N-formyltetrahydrofolate as the carbon source. Kinetic analyses demonstrate that Rv3404c displays a significant catalytic efficiency of 1.1 × 10 M s. In addition, we report the X-ray structure of a ternary complex of Rv3404c solved in the presence of N-formyltetrahydrofolate and dTDP-4-amino-4,6-dideoxyglucose. The final model of Rv3404c was refined to an overall R-factor of 16.8% at 1.6 Å resolution. The results described herein are especially intriguing given that there have been no published reports of N-formylated sugars associated with M. tuberculosis. The data thus provide a new avenue of research into this fascinating, yet deadly, organism that apparently has been associated with human infection since ancient times.

PubMed: 28665588
DOI: 10.1021/acs.biochem.7b00506

Experimental method

X-RAY DIFFRACTION (1.6 Å)