3a76 | pdb_00003a76

The crystal structure of LinA

spinqualitylabelsall models 3a76, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3a76 is a 3 chain structure with sequence from "bacillus_devorans"_zimmermann_1890 "bacillus devorans" zimmermann 1890. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, SPD Gene: linA ("Bacillus devorans" Zimmermann 1890) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LINA_SPHPI] Catalyzes the conversion of the important environmental pollutant gamma-hexachlorocyclohexane (gamma-HCH or lindane) to 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) via gamma-pentachlorocyclohexene (gamma-PCCH), proceeding by two successive 1,2-anti conformationally dependent dehydrochlorinations. Also shows activity with alpha- and delta-HCH, giving alpha- and delta-PCCH respectively, but not with the beta isomer. 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 LinA from Sphingobium japonicum UT26 catalyzes two steps of dehydrochlorination from gamma hexachlorocyclohexane (HCH) to 1,3,4,6-tetrachloro-1,4-cyclohexadiene via gamma-pentachlorocyclohexene. We determined the crystal structure of LinA at 2.25 A by single anomalous dispersion. LinA exists as a homotrimer, and each protomer forms a cone-shaped alpha+beta barrel fold. The C-terminal region of LinA is extended to the neighboring subunit, unlike that of scytalone dehydratase from Magnaporthe grisea, which is one of the most structurally similar proteins identified by the DALI server. The structure we obtained in this study is in open form, in which gamma-HCH can enter the active site. There is a hydrophobic cavity inside the barrel fold, and the active site is largely surrounded by the side chains of K20, L21, V24, D25, W42, L64, F68, C71, H73, V94, L96, I109, F113, and R129. H73 was considered to function as a base that abstracts the proton of gamma-HCH through its interaction with D25. Docking simulations with gamma-HCH, gamma-pentachlorocyclohexene, (+)-alpha-HCH, and (-)-alpha-HCH suggest that 11 residues (K20, I44, L64, V94, L96, I109, A111, F113, A131, C132, and T133) are involved in the binding of these compounds and support enantiomeric preference and the degradation mechanism. Crystal Structure of gamma-Hexachlorocyclohexane Dehydrochlorinase LinA from Sphingobium japonicum UT26.,Okai M, Kubota K, Fukuda M, Nagata Y, Nagata K, Tanokura M J Mol Biol. 2010 Sep 7. PMID:20813114 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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