7OY9

Crystal structure of GMP reductase from mycobacterium smegmatis.

Summary for 7OY9

• Entry DOI: 10.2210/pdb7oy9/pdb
• Descriptor: Guanosine 5'-monophosphate reductase (1 entity in total)
• Functional Keywords: gmp reductase gmpr oxidoreductase guab1 octamer cbs domain bateman domain mycobacterium smegmatis, oxidoreductase
• Biological source: Mycolicibacterium smegmatis
• Total number of polymer chains: 8
• Total formula weight: 414259.47

Authors

Dolezal, M.,Klima, M.,Pichova, I. (deposition date: 2021-06-24, release date: 2022-04-27, Last modification date: 2024-01-31)

Primary citation

Knejzlik, Z.,Dolezal, M.,Herkommerova, K.,Clarova, K.,Klima, M.,Dedola, M.,Zbornikova, E.,Rejman, D.,Pichova, I.
The mycobacterial guaB1 gene encodes a guanosine 5'-monophosphate reductase with a cystathionine-beta-synthase domain.
Febs J., 289:5571-5598, 2022

PubMed Abstract: Mycobacteria express enzymes from both the de novo and purine-salvage pathways. However, the regulation of these processes and the roles of individual metabolic enzymes have not been sufficiently detailed. Both Mycobacterium tuberculosis (Mtb) and Mycobacterium smegmatis (Msm) possess three guaB genes, but information is only available on guaB2, which encodes an essential inosine 5'-monophosphate dehydrogenase (IMPDH) involved in de novo purine biosynthesis. This study shows that guaB1, annotated in databases as a putative IMPDH, encodes a guanosine 5'-monophosphate reductase (GMPR), which recycles guanosine monophosphate to inosine monophosphate within the purine-salvage pathway and contains a cystathionine-β-synthase domain (CBS), which is essential for enzyme activity. GMPR activity is allosterically regulated by the ATP/GTP ratio in a pH-dependent manner. Bioinformatic analysis has indicated the presence of GMPRs containing CBS domains across the entire Actinobacteria phylum.

PubMed: 35338694
DOI: 10.1111/febs.16448

Experimental method

X-RAY DIFFRACTION (2.8 Å)