1BFD

BENZOYLFORMATE DECARBOXYLASE FROM PSEUDOMONAS PUTIDA

1BFD の概要

• エントリーDOI: 10.2210/pdb1bfd/pdb
• 分子名称: BENZOYLFORMATE DECARBOXYLASE, CALCIUM ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: lyase, carbon-carbon, decarboxylase, mandelate catabolism, thiamin diphosphate
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56932.52

構造登録者

Hasson, M.S.,Muscate, A.,Mcleish, M.J.,Polovnikova, L.S.,Gerlt, J.A.,Kenyon, G.L.,Petsko, G.A.,Ringe, D. (登録日: 1998-04-30, 公開日: 1998-06-24, 最終更新日: 2024-02-07)

主引用文献

Hasson, M.S.,Muscate, A.,McLeish, M.J.,Polovnikova, L.S.,Gerlt, J.A.,Kenyon, G.L.,Petsko, G.A.,Ringe, D.
The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes.
Biochemistry, 37:9918-9930, 1998

PubMed Abstract: The crystal structure of the thiamin diphosphate (ThDP)-dependent enzyme benzoylformate decarboxylase (BFD), the third enzyme in the mandelate pathway of Pseudomonas putida, has been solved by multiple isomorphous replacement at 1.6 A resolution and refined to an R-factor of 15.0% (free R = 18.6%). The structure of BFD has been compared to that of other ThDP-dependent enzymes, including pyruvate decarboxylase. The overall architecture of BFD resembles that of the other family members, and cofactor- and metal-binding residues are well conserved. Surprisingly, there is no conservation of active-site residues not directly bound to the cofactor. The position of functional groups in the active site may be conserved, however. Three classes of metal ions have been identified in the BFD crystal structure: Ca2+ bound to the cofactor in each subunit, Mg2+ on a 2-fold axis of the tetramer, and Ca2+ at a crystal contact. The structure includes a non-proline cis-peptide bond and an unusually long and regular polyproline type II helix that mediates the main contact between tetramers in the crystal. The high-quality electron-density map allowed the correction of errors totaling more than 10% of the amino acid sequence, which had been predicted from the reported sequence of the mdlC gene. Analysis of the BFD structure suggests that requirements for activation of the cofactor, the nature of the reaction intermediates, and architectural considerations relating to the protein fold have been dominant forces in the evolution of ThDP-dependent enzymes.

PubMed: 9665697
DOI: 10.1021/bi973047e

実験手法

X-RAY DIFFRACTION (1.6 Å)