7CIM

Crystal structure of L-methionine decarboxylase from Streptomyces sp.590 in complexed with 3-methlythiopropylamine (geminal diamine form).

7CIM の概要

• エントリーDOI: 10.2210/pdb7cim/pdb
• 分子名称: L-methionine decarboxylase, [6-methyl-4-[(3-methylsulfanylpropylamino)methyl]-5-oxidanyl-pyridin-3-yl]methyl dihydrogen phosphate (3 entities in total)
• 機能のキーワード: decarboxylase, plp-dependent enzymes, lyase
• 由来する生物種: Streptomyces sp. 590 KI-2014
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 123626.88

構造登録者

Okawa, A.,Shiba, T.,Hayashi, M.,Onoue, Y.,Murota, M.,Sato, D.,Inagaki, J.,Tamura, T.,Harada, S.,Inagaki, K. (登録日: 2020-07-07, 公開日: 2021-01-27, 最終更新日: 2024-10-30)

主引用文献

Okawa, A.,Shiba, T.,Hayashi, M.,Onoue, Y.,Murota, M.,Sato, D.,Inagaki, J.,Tamura, T.,Harada, S.,Inagaki, K.
Structural basis for substrate specificity of l-methionine decarboxylase.
Protein Sci., 30:663-677, 2021

PubMed Abstract: l -Methionine decarboxylase (MetDC) from Streptomyces sp. 590 is a vitamin B -dependent enzyme and catalyzes the non-oxidative decarboxylation of l -methionine to produce 3-methylthiopropylamine and carbon dioxide. We present here the crystal structures of the ligand-free form of MetDC and of several enzymatic reaction intermediates. Group II amino acid decarboxylases have many residues in common around the active site but the residues surrounding the side chain of the substrate differ. Based on information obtained from the crystal structure, and mutational and biochemical experiments, we propose a key role for Gln64 in determining the substrate specificity of MetDC, and for Tyr421 as the acid catalyst that participates in protonation after the decarboxylation reaction.

PubMed: 33452696
DOI: 10.1002/pro.4027

実験手法

X-RAY DIFFRACTION (1.8 Å)