2BOY

Crystal structure of 3-ChloroCatechol 1,2-Dioxygenase from Rhodococcus Opacus 1CP

2BOY の概要

• エントリーDOI: 10.2210/pdb2boy/pdb
• 分子名称: 3-CHLOROCATECHOL 1,2-DIOXYGENASE, FE (III) ION, BENZHYDROXAMIC ACID, ... (6 entities in total)
• 機能のキーワード: beta barrel, oxidoreductase, dioxygenase
• 由来する生物種: RHODOCOCCUS OPACUS
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 232176.33

構造登録者

Ferraroni, M.,Solyanikova, I.P.,Kolomytseva, M.P.,Scozzafava, A.,Golovleva, L.A.,Briganti, F. (登録日: 2005-04-15, 公開日: 2006-08-24, 最終更新日: 2023-12-13)

主引用文献

Ferraroni, M.,Kolomytseva, M.P.,Solyanikova, I.P.,Scozzafava, A.,Golovleva, L.A.,Briganti, F.
Crystal structure of 3-chlorocatechol 1,2-dioxygenase key enzyme of a new modified ortho-pathway from the Gram-positive Rhodococcus opacus 1CP grown on 2-chlorophenol.
J. Mol. Biol., 360:788-799, 2006

PubMed Abstract: The crystal structure of the 3-chlorocatechol 1,2-dioxygenase from the Gram-positive bacterium Rhodococcus opacus (erythropolis) 1CP, a Fe(III) ion-containing enzyme specialized in the aerobic biodegradation of 3-chloro- and methyl-substituted catechols, has been solved by molecular replacement techniques using the coordinates of 4-chlorocatechol 1,2-dioxygenase from the same organism (PDB code 1S9A) as a starting model and refined at 1.9 A resolution (R(free) 21.9%; R-factor 17.4%). The analysis of the structure and of the kinetic parameters for a series of different substrates, and the comparison with the corresponding data for the 4-chlorocatechol 1,2-dioxygenase isolated from the same bacterial strain, provides evidence of which active site residues are responsible for the observed differences in substrate specificity. Among the amino acid residues expected to interact with substrates, only three are altered Val53(Ala53), Tyr78(Phe78) and Ala221(Cys224) (3-chlorocatechol 1,2-dioxygenase(4-chlorocatechol 1,2-dioxygenase)), clearly identifying the substitutions influencing substrate selectivity in these enzymes. The crystallographic asymmetric unit contains eight subunits (corresponding to four dimers) that show heterogeneity in the conformation of a co-crystallized molecule bound to the catalytic non-heme iron(III) ion resembling a benzohydroxamate moiety, probably a result of the breakdown of recently discovered siderophores synthesized by Gram-positive bacteria. Several different modes of binding benzohydroxamate into the active site induce distinct conformations of the interacting protein ligands Tyr167 and Arg188, illustrating the plasticity of the active site origin of the more promiscuous substrate preferences of the present enzyme.

PubMed: 16793061
DOI: 10.1016/j.jmb.2006.05.046

実験手法

X-RAY DIFFRACTION (1.9 Å)