3x16

Crystal structure of the catalase-peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942

spinqualitylabelsall models 3x16, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3x16 is a 1 chain structure with sequence from Synechococcus elongatus PCC 7942 = FACHB-805. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.65Å Ligands: HEB, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KATG_SYNE7 Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.[HAMAP-Rule:MF_01961] Publication Abstract from PubMed Isoniazid (INH) is a pro-drug that has been extensively used to treat tuberculosis. INH is activated by the heme enzyme catalase-peroxidase (KatG), but the mechanism of the activation is poorly understood, in part because the INH binding site has not been clearly established. Here, we observed that a single-residue mutation of KatG from Synechococcus elongatus PCC7942 (SeKatG), W78F, enhances INH activation. The crystal structure of INH-bound KatG-W78F revealed that INH binds to the heme pocket. The results of a thermal-shift assay implied that the flexibility of the SeKatG molecule is increased by the W78F mutation, allowing the INH molecule to easily invade the heme pocket through the access channel on the gamma-edge side of the heme. Crystal structure of the catalase-peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942 in complex with the antitubercular pro-drug isoniazid.,Kamachi S, Hirabayashi K, Tamoi M, Shigeoka S, Tada T, Wada K FEBS Lett. 2015 Jan 2;589(1):131-7. doi: 10.1016/j.febslet.2014.11.037. Epub 2014, Dec 3. PMID:25479089 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Catalase 3D structures

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