6KHR

Structure of glycinamide-RNase-transformylase T from Mycobacterium tuberculosis

Summary for 6KHR

• Entry DOI: 10.2210/pdb6khr/pdb
• Descriptor: Formate-dependent phosphoribosylglycinamide formyltransferase (2 entities in total)
• Functional Keywords: purine salvag pathway, transferase
• Biological source: Mycobacterium tuberculosis H37Rv
• Total number of polymer chains: 2
• Total formula weight: 87631.27

Authors

Chen, C.,Wang, J. (deposition date: 2019-07-16, release date: 2019-12-18, Last modification date: 2023-11-22)

Primary citation

Chen, C.,Liu, Z.,Liu, L.,Wang, J.,Jin, Q.
Structural characterization of glycinamide-RNase-transformylase T fromMycobacterium tuberculosis.
Emerg Microbes Infect, 9:58-66, 2020

PubMed Abstract: Enzymes from the purine salvage pathway in () have been regarded as an attractive target for the development of anti-bacterial drugs. Although this pathway has not been extensively studied in , it has been identified as essential for growth and survival. Glycinamide-RNase-transformylase T (PurT) is found only in some specific bacteria including and utilizes ATP-dependent ligation to catalyze the formylation of 5'-phosphoribosyl-glycinamide (GAR) in the third reaction of the de novo purine salvage pathway. In the study, we determined the crystal structure of PurT at a resolution of 2.79 Å. In contrast to PurT (phBCCPPurT), PurT exhibits an "open" conformation, which results in a broader ATP-binding pocket and thus might facilitate the entry and exit of the cofactor. Additionally, active site superposition with PurT (PurT) showed that residues involved in the ATP-binding site in PurT exhibited structural similarity but had notable difference in the GAR-binding site. The loop 383-389 in PurT was much shorter and shifted 5.7 Å away from the phosphate of the GAR substrate. The different GAR-binding mode might result in a large conformational change in PurT, and would provide a possible opportunity for anti-TB drug development.

PubMed: 31894729
DOI: 10.1080/22221751.2019.1707716

Experimental method

X-RAY DIFFRACTION (2.786 Å)