2WBP

Crystal structure of VioC in complex with Fe(II), (2S,3S)- hydroxyarginine, and succinate

2WBP の概要

• エントリーDOI: 10.2210/pdb2wbp/pdb
• 関連するPDBエントリー: 2WBO 2WBQ
• 分子名称: L-ARGININE BETA-HYDROXYLASE, ARGININE, FE (II) ION, ... (7 entities in total)
• 機能のキーワード: oxidoreductase, non-heme fe(ii) hydroxylase, cbeta-hydroxylation, nrps, viomycin, alpha-ketoglutarate
• 由来する生物種: STREPTOMYCES VINACEUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40112.64

構造登録者

Helmetag, V.,Samel, S.A.,Thomas, M.G.,Marahiel, M.A.,Essen, L.-O. (登録日: 2009-03-02, 公開日: 2009-06-23, 最終更新日: 2023-12-13)

主引用文献

Helmetag, V.,Samel, S.A.,Thomas, M.G.,Marahiel, M.A.,Essen, L.-O.
Structural Basis for the Erythro-Stereospecificity of the L-Arginine Oxygenase Vioc in Viomycin Biosynthesis.
FEBS J., 276:3669-, 2009

PubMed Abstract: The nonheme iron oxygenase VioC from Streptomyces vinaceus catalyzes Fe(II)-dependent and alpha-ketoglutarate-dependent Cbeta-hydroxylation of L-arginine during the biosynthesis of the tuberactinomycin antibiotic viomycin. Crystal structures of VioC were determined in complexes with the cofactor Fe(II), the substrate L-arginine, the product (2S,3S)-hydroxyarginine and the coproduct succinate at 1.1-1.3 A resolution. The overall structure reveals a beta-helix core fold with two additional helical subdomains that are common to nonheme iron oxygenases of the clavaminic acid synthase-like superfamily. In contrast to other clavaminic acid synthase-like oxygenases, which catalyze the formation of threo diastereomers, VioC produces the erythro diastereomer of Cbeta-hydroxylated L-arginine. This unexpected stereospecificity is caused by conformational control of the bound substrate, which enforces a gauche(-) conformer for chi(1) instead of the trans conformers observed for the asparagine oxygenase AsnO and other members of the clavaminic acid synthase-like superfamily. Additionally, the substrate specificity of VioC was investigated. The side chain of the L-arginine substrate projects outwards from the active site by undergoing interactions mainly with the C-terminal helical subdomain. Accordingly, VioC exerts broadened substrate specificity by accepting the analogs L-homoarginine and L-canavanine for Cbeta-hydroxylation.

PubMed: 19490124
DOI: 10.1111/J.1742-4658.2009.07085.X

実験手法

X-RAY DIFFRACTION (1.16 Å)