6S83

Crystal structure of methionine adenosyltransferase from Pyrococcus furiosus in complex with AMPPCP, SAM, and PCP

6S83 の概要

• エントリーDOI: 10.2210/pdb6s83/pdb
• 関連するPDBエントリー: 6S81
• 分子名称: S-adenosylmethionine synthase, METHYLENEDIPHOSPHONIC ACID, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: s-adenosyl methionine synthesis, cofactor biosynthesis, transferase, cytoplasmic
• 由来する生物種: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 359501.17

構造登録者

Degano, M.,Minici, C.,Porcelli, M. (登録日: 2019-07-08, 公開日: 2020-02-05, 最終更新日: 2024-01-24)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.336 Å)