8A8G

ATP sulfurylase from Methanothermococcus thermolithotrophicus - orthorhombic form

Summary for 8A8G

• Entry DOI: 10.2210/pdb8a8g/pdb
• Descriptor: ATP sulfurylase from Methanothermococcus thermolithotrophicus, GLYCEROL, ZINC ION, ... (4 entities in total)
• Functional Keywords: sulfate assimilation, methanogens, archaea, aps, atp, thermophile, transferase, methane, activation, marine
• Biological source: Methanothermococcus thermolithotrophicus DSM 2095
• Total number of polymer chains: 1
• Total formula weight: 45521.92

Authors

Jespersen, M.,Wagner, T. (deposition date: 2022-06-23, release date: 2023-04-26, Last modification date: 2024-02-07)

Primary citation

Jespersen, M.,Wagner, T.
Assimilatory sulfate reduction in the marine methanogen Methanothermococcus thermolithotrophicus.
Nat Microbiol, 8:1227-1239, 2023

PubMed Abstract: Methanothermococcus thermolithotrophicus is the only known methanogen that grows on sulfate as its sole sulfur source, uniquely uniting methanogenesis and sulfate reduction. Here we use physiological, biochemical and structural analyses to provide a snapshot of the complete sulfate reduction pathway of this methanogenic archaeon. We find that later steps in this pathway are catalysed by atypical enzymes. PAPS (3'-phosphoadenosine 5'-phosphosulfate) released by APS kinase is converted into sulfite and 3'-phosphoadenosine 5'-phosphate (PAP) by a PAPS reductase that is similar to the APS reductases of dissimilatory sulfate reduction. A non-canonical PAP phosphatase then hydrolyses PAP. Finally, the F-dependent sulfite reductase converts sulfite to sulfide for cellular assimilation. While metagenomic and metatranscriptomic studies suggest that the sulfate reduction pathway is present in several methanogens, the sulfate assimilation pathway in M. thermolithotrophicus is distinct. We propose that this pathway was 'mix-and-matched' through the acquisition of assimilatory and dissimilatory enzymes from other microorganisms and then repurposed to fill a unique metabolic role.

PubMed: 37277534
DOI: 10.1038/s41564-023-01398-8

Experimental method

X-RAY DIFFRACTION (1.97 Å)