6TNH

Deoxyguanylosuccinate synthase (DgsS) quaternary structure with AMPPcP, dGMP, Asp, Magnesium at 2.21 Angstrom resolution

Summary for 6TNH

• Entry DOI: 10.2210/pdb6tnh/pdb
• Descriptor: Adenylosuccinate synthetase, SULFATE ION, 2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE, ... (7 entities in total)
• Functional Keywords: 2, 6-diaminopurine, phage phivc8, synthetase, biosynthetic protein
• Biological source: Vibrio phage phiVC8
• Total number of polymer chains: 2
• Total formula weight: 83537.12

Authors

Sleiman, D.,Loc'h, J.,Haouz, A.,Kaminski, P.A. (deposition date: 2019-12-08, release date: 2020-12-16, Last modification date: 2024-01-24)

Primary citation

Sleiman, D.,Garcia, P.S.,Lagune, M.,Loc'h, J.,Haouz, A.,Taib, N.,Rothlisberger, P.,Gribaldo, S.,Marliere, P.,Kaminski, P.A.
A third purine biosynthetic pathway encoded by aminoadenine-based viral DNA genomes.
Science, 372:516-520, 2021

PubMed Abstract: Cells have two purine pathways that synthesize adenine and guanine ribonucleotides from phosphoribose via inosylate. A chemical hybrid between adenine and guanine, 2-aminoadenine (Z), replaces adenine in the DNA of the cyanobacterial virus S-2L. We show that S-2L and phage PhiVC8 encode a third purine pathway catalyzed by PurZ, a distant paralog of succinoadenylate synthase (PurA), the enzyme condensing aspartate and inosylate in the adenine pathway. PurZ condenses aspartate with deoxyguanylate into dSMP (N6-succino-2-amino-2'-deoxyadenylate), which undergoes defumarylation and phosphorylation to give dZTP (2-amino-2'-deoxyadenosine-5'-triphosphate), a substrate for the phage DNA polymerase. Crystallography and phylogenetics analyses indicate a close relationship between phage PurZ and archaeal PurA enzymes. Our work elucidates the biocatalytic innovation that remodeled a DNA building block beyond canonical molecular biology.

PubMed: 33926955
DOI: 10.1126/science.abe6494

Experimental method

X-RAY DIFFRACTION (2.21 Å)