5MP7

Crystal structure of phosphoribosylpyrophosphate synthetase from Mycobacterium smegmatis

Summary for 5MP7

• Entry DOI: 10.2210/pdb5mp7/pdb
• Descriptor: Ribose-phosphate pyrophosphokinase, ACETATE ION (3 entities in total)
• Functional Keywords: phosphoribosylpyrophosphate synthetase, prpp synthetase, mycobacterium smegmatis, transferase
• Biological source: Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
• Total number of polymer chains: 3
• Total formula weight: 106987.82

Authors

Donini, S.,Garavaglia, S.,Ferraris, D.M.,Miggiano, R.,Mori, S.,Shibayama, K.,Rizzi, M. (deposition date: 2016-12-16, release date: 2017-04-26, Last modification date: 2024-01-17)

Primary citation

Donini, S.,Garavaglia, S.,Ferraris, D.M.,Miggiano, R.,Mori, S.,Shibayama, K.,Rizzi, M.
Biochemical and structural investigations on phosphoribosylpyrophosphate synthetase from Mycobacterium smegmatis.
PLoS ONE, 12:e0175815-e0175815, 2017

PubMed Abstract: Mycobacterium smegmatis represents one model for studying the biology of its pathogenic relative Mycobacterium tuberculosis. The structural characterization of a M. tuberculosis ortholog protein can serve as a valid tool for the development of molecules active against the M. tuberculosis target. In this context, we report the biochemical and structural characterization of M. smegmatis phosphoribosylpyrophosphate synthetase (PrsA), the ortholog of M. tuberculosis PrsA, the unique enzyme responsible for the synthesis of phosphoribosylpyrophosphate (PRPP). PRPP is a key metabolite involved in several biosynthetic pathways including those for histidine, tryptophan, nucleotides and decaprenylphosphoryl-arabinose, an essential precursor for the mycobacterial cell wall biosynthesis. Since M. tuberculosis PrsA has been validated as a drug target for the development of antitubercular agents, the data presented here will add to the knowledge of the mycobacterial enzyme and could contribute to the development of M. tuberculosis PrsA inhibitors of potential pharmacological interest.

PubMed: 28419153
DOI: 10.1371/journal.pone.0175815

Experimental method

X-RAY DIFFRACTION (2.4 Å)