2wl3

CRYSTAL STRUCTURE OF CATECHOL 2,3-DIOXYGENASE

spinqualitylabelsall models 2wl3, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wl3 is a 4 chain structure with sequence from Rhodococcus sp. dk17. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, FE, GOL NonStd Res: MSE Related: 2wl9 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed A meta-cleavage pathway for the aerobic degradation of aromatic hydrocarbons is catalyzed by extradiol dioxygenases via a two-step mechanism: catechol substrate binding and dioxygen incorporation. The binding of substrate triggers the release of water, thereby opening a coordination site for molecular oxygen. The crystal structures of AkbC, a type I extradiol dioxygenase, and the enzyme-substrate (3-methylcatechol) complex revealed the substrate-binding process of extradiol dioxygenase. AkbC is composed of an N-domain and an active C-domain, which contains iron coordinated by a 2-His-1-carboxylate facial triad motif. The C-domain includes a beta-hairpin structure and a C-terminal tail. In substrate-bound AkbC, 3-methylcatechol interacts with the iron via a single hydroxyl group, which represents an intermediate stage in the substrate-binding process. Structure-based mutagenesis revealed that the C-terminal tail and beta-hairpin form part of the substrate-binding pocket that is responsible for substrate specificity by blocking substrate entry. Once a substrate enters the active site, these structural elements also play a role in the correct positioning of the substrate. Based on the results presented here, a putative substrate-binding mechanism is proposed. Substrate-binding mechanism of a type I extradiol dioxygenase.,Cho HJ, Kim K, Sohn SY, Cho HY, Kim KJ, Kim MH, Kim D, Kim E, Kang BS J Biol Chem. 2010 Sep 1. PMID:20810655 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dioxygenase

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