3X43

Crystal structure of O-ureido-L-serine synthase

3X43 の概要

• エントリーDOI: 10.2210/pdb3x43/pdb
• 分子名称: O-ureido-L-serine synthase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: d-cycloserine, type ii plp enzyme, synthase, transferase
• 由来する生物種: Streptomyces lavendulae
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 287580.35

構造登録者

Matoba, Y.,Uda, N.,Oda, K.,Sugiyama, M. (登録日: 2015-03-13, 公開日: 2015-07-29, 最終更新日: 2023-11-08)

主引用文献

Uda, N.,Matoba, Y.,Oda, K.,Kumagai, T.,Sugiyama, M.
The structural and mutational analyses of O-ureido-L-serine synthase necessary for D-cycloserine biosynthesis.
Febs J., 282:3929-3944, 2015

PubMed Abstract: We have recently been successful in cloning a gene cluster necessary for the biosynthesis of D-cycloserine (D-CS) from D-CS-producing Streptomyces lavendulae ATCC11924. Although dcsD, one of the ORFs located on the gene cluster, encodes a protein homologous to O-acetylserine sulfhydrylase that synthesizes L-cysteine using O-acetyl-L-serine together with sulfide, it functions to form O-ureido-L-serine as a D-CS biosynthetic intermediate, using O-acetyl-L-serine together with hydroxyurea (HU). In the present study, using crystallographic and mutational studies, three amino acid residues in DcsD that are important for the substrate preference toward HU were determined. We showed that two of the three residues are important for the binding of HU into the substrate-binding pocket. The other residue contributes to the formation of a loose hydrogen-bond network during the catalytic reaction. Information regarding the amino acid residues will be very useful in the design of a new catalyst for synthesizing the β-substituted-L-alanine derivatives.

PubMed: 26207937
DOI: 10.1111/febs.13386

実験手法

X-RAY DIFFRACTION (2.25 Å)