5A1G

The structure of Human MAT2A in complex with S-adenosylethionine and PPNP.

5A1G の概要

• エントリーDOI: 10.2210/pdb5a1g/pdb
• 関連するPDBエントリー: 5A19 5A1I
• 分子名称: S-ADENOSYLMETHIONINE SYNTHASE ISOFORM TYPE-2, (4S)-2-METHYL-2,4-PENTANEDIOL, (DIPHOSPHONO)AMINOPHOSPHONIC ACID, ... (8 entities in total)
• 機能のキーワード: transferase, methionine adenosyltransferase, cell growth, liver cancer, methylation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44784.21

構造登録者

Murray, B.,Antonyuk, S.V.,Marina, A.,Lu, S.C.,Mato, J.M.,Hasnain, S.S.,Rojas, A.L. (登録日: 2015-04-30, 公開日: 2016-02-17, 最終更新日: 2024-01-10)

主引用文献

Murray, B.,Antonyuk, S.V.,Marina, A.,Lu, S.C.,Mato, J.M.,Hasnain, S.S.,Rojas, A.L.
Crystallography Captures Catalytic Steps in Human Methionine Adenosyltransferase Enzymes.
Proc.Natl.Acad.Sci.USA, 113:2104-, 2016

PubMed Abstract: The principal methyl donor of the cell, S-adenosylmethionine (SAMe), is produced by the highly conserved family of methionine adenosyltranferases (MATs) via an ATP-driven process. These enzymes play an important role in the preservation of life, and their dysregulation has been tightly linked to liver and colon cancers. We present crystal structures of human MATα2 containing various bound ligands, providing a "structural movie" of the catalytic steps. High- to atomic-resolution structures reveal the structural elements of the enzyme involved in utilization of the substrates methionine and adenosine and in formation of the product SAMe. MAT enzymes are also able to produce S-adenosylethionine (SAE) from substrate ethionine. Ethionine, an S-ethyl analog of the amino acid methionine, is known to induce steatosis and pancreatitis. We show that SAE occupies the active site in a manner similar to SAMe, confirming that ethionine also uses the same catalytic site to form the product SAE.

PubMed: 26858410
DOI: 10.1073/PNAS.1510959113

実験手法

X-RAY DIFFRACTION (1.83 Å)