4WXB

Crystal Structure of Serine Hydroxymethyltransferase from Streptococcus thermophilus

4WXB の概要

• エントリーDOI: 10.2210/pdb4wxb/pdb
• 分子名称: Serine hydroxymethyltransferase, CITRIC ACID, CACODYLATE ION, ... (6 entities in total)
• 機能のキーワード: aldolase, serine hydrodymethyltransferase, transferase, aldehydes, catalysis, catalytic domain, escherichia coli, chemical, protein binding, protein conformation, protein structure
• 由来する生物種: Streptococcus thermophilus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 187927.97

構造登録者

Hernandez, K.,Zelen, I.,Petrillo, G.,Uson, I.,Wandtke, C.,Bujons, J.,Joglar, J.,Parella, T.,Clapes, P. (登録日: 2014-11-13, 公開日: 2015-02-04, 最終更新日: 2024-01-10)

主引用文献

Hernandez, K.,Zelen, I.,Petrillo, G.,Uson, I.,Wandtke, C.M.,Bujons, J.,Joglar, J.,Parella, T.,Clapes, P.
Engineered L-Serine Hydroxymethyltransferase from Streptococcus thermophilus for the Synthesis of alpha , alpha-Dialkyl-alpha-Amino Acids.
Angew.Chem.Int.Ed.Engl., 54:3013-3017, 2015

PubMed Abstract: α,α-Disubstituted α-amino acids are central to biotechnological and biomedical chemical processes for their own sake and as substructures of biologically active molecules for diverse biomedical applications. Structurally, these compounds contain a quaternary stereocenter, which is particularly challenging for stereoselective synthesis. The pyridoxal-5'-phosphate (PLP)-dependent L-serine hydroxymethyltransferase from Streptococcus thermophilus (SHMT(Sth); EC 2.1.2.1) was engineered to achieve the stereoselective synthesis of a broad structural variety of α,α-dialkyl-α-amino acids. This was accomplished by the formation of quaternary stereocenters through aldol addition of the amino acids D-Ala and D-Ser to a wide acceptor scope catalyzed by the minimalist SHMT(Sth) Y55T variant overcoming the limitation of the native enzyme for Gly. The SHMT(Sth) Y55T variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors.

PubMed: 25611820
DOI: 10.1002/anie.201411484

実験手法

X-RAY DIFFRACTION (2.05 Å)