6S81

Crystal structure of methionine adenosyltransferase from Pyrococcus furiosus

Summary for 6S81

• Entry DOI: 10.2210/pdb6s81/pdb
• Descriptor: S-adenosylmethionine synthase, MANGANESE (II) ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: s-adenosyl methionine synthesis, cofactor biosynthesis, transferase, cytoplasmic
• Biological source: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
• Total number of polymer chains: 4
• Total formula weight: 178106.68

Authors

Degano, M.,Minici, C.,Porcelli, M. (deposition date: 2019-07-08, release date: 2020-02-05, Last modification date: 2024-01-24)

Primary citation

Minici, C.,Mosca, L.,Ilisso, C.P.,Cacciapuoti, G.,Porcelli, M.,Degano, M.
Structures of catalytic cycle intermediates of the Pyrococcus furiosus methionine adenosyltransferase demonstrate negative cooperativity in the archaeal orthologues.
J.Struct.Biol., 210:107462-107462, 2020

PubMed Abstract: Methionine adenosyltransferases catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions, through the condensation of methionine and ATP. Here, we report the structural analysis of the Pyrococcus furiosus methionine adenosyltransferase (PfMAT) captured in the unliganded, substrate- and product-bound states. The conformational changes taking place during the enzymatic catalytic cycle are allosterically propagated by amino acid residues conserved in the archaeal orthologues to induce an asymmetric dimer structure. The distinct occupancy of the active sites within a PfMAT dimer is consistent with a half-site reactivity that is mediated by a product-induced negative cooperativity. The structures of intermediate states of PfMAT reported here suggest a distinct molecular mechanism for S-adenosylmethionine synthesis in Archaea, likely consequence of the evolutionary pressure to achieve protein stability under extreme conditions.

PubMed: 31962159
DOI: 10.1016/j.jsb.2020.107462

Experimental method

X-RAY DIFFRACTION (1.784 Å)