3U4C

Crystal structure of YwfH, NADPH dependent reductase involved in Bacilysin biosynthesis

3U4C の概要

• エントリーDOI: 10.2210/pdb3u4c/pdb
• 関連するPDBエントリー: 3U49 3U4D
• 分子名称: Bacilysin biosynthesis oxidoreductase ywfH, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: nadph binding motif, rossmann fold, sdr superfamily, oxidoreductase, bacilysin biosynthesis
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm : P39644
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31211.04

構造登録者

Rajavel, M.,Gopal, B. (登録日: 2011-10-07, 公開日: 2013-03-06, 最終更新日: 2024-03-20)

主引用文献

Rajavel, M.,Perinbam, K.,Gopal, B.
Structural insights into the role of Bacillus subtilis YwfH (BacG) in tetrahydrotyrosine synthesis
Acta Crystallogr.,Sect.D, 69:324-332, 2013

PubMed Abstract: The synthesis of the dipeptide antibiotic bacilysin involves the sequential action of multiple enzymes in the bac operon. YwfH (also referred to as BacG) catalyzes the stereoselective reduction of dihydro-hydroxyphenylpyruvate (H2HPP) to tetrahydro-hydroxyphenylpyruvate (H4HPP) in this biosynthetic pathway. YwfH is an NADPH-dependent reductase that facilitates the conjugate addition of a hydride at the C4 olefin terminus of H2HPP. Here, the structure of YwfH is described at three conformational steps: the apo form, an apo-like conformation and the NADPH complex. YwfH is structurally similar to other characterized short-chain dehydrogenase/reductases despite having marginal sequence similarity. The structures of YwfH in different conformational states provide a rationale for the ping-pong reaction mechanism. The identification and role of the residues in the catalytic tetrad (Lys113-Tyr117-Ser155-Asn158) in proton transfer were examined by mutational analysis. Together, the structures and biochemical features revealed synchronized conformational changes that facilitate cofactor specificity and catalysis of H4HPP formation en route to tetrahydrotyrosine synthesis.

PubMed: 23519407
DOI: 10.1107/S0907444912046690

実験手法

X-RAY DIFFRACTION (2.03 Å)