4bjz

Crystal structure of 3-hydroxybenzoate 6-hydroxylase uncovers lipid- assisted flavoprotein strategy for regioselective aromatic hydroxylation: Native data

spinqualitylabelsall models 4bjz, resolution 1.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bjz is a 1 chain structure with sequence from Rhodococcus jostii RHA1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.51Å Ligands: CL, FAD, P3A Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q0SFK6_RHOJR Publication Abstract from PubMed 3-Hydroxybenzoate hydroxylase from Rhodococcus jostii RHA1 (3HB6H) is a dimeric flavoprotein that catalyses the NADH- and oxygen-dependent para-hydroxylation of 3 hydroxybenzoate to 2,5-dihydroxybenzoate. In this study, we report the crystal structure of 3HB6H, as expressed in Escherichia coli. The overall fold of 3HB6H is similar to that of p- hydroxybenzoate hydroxylase (PHBH) and other flavoprotein aromatic hydroxylases. Unexpectedly, a lipid ligand is bound to each 3HB6H monomer. Mass spectral analysis identifies the ligand as a mixture of phosphatidylglycerol and phosphatidylethanolamine. The fatty acid chains occupy hydrophobic channels that deeply penetrate into the interior of the substrate-binding domain of each subunit, whereas the hydrophilic part is exposed on the protein surface, connecting the dimerization domains via few interactions. Most remarkably, the terminal part of a phospholipid acyl chain is directly involved in the substrate-binding site. Co-crystallized chloride ion and the crystal structure of the His213Ser variant with bound 3-hydroxybenzoate provide hints about oxygen activation and substrate hydroxylation. Essential roles are played by His213 in catalysis and Tyr105 in substrate binding. This phospholipid-assisted strategy to control regioselective aromatic hydroxylation is of relevance for optimization of flavin-dependent biocatalysts. Crystal structure of 3-hydroxybenzoate 6-hydroxylase uncovers lipid-assisted flavoprotein strategy for regioselective aromatic hydroxylation.,Montersino S, Orru R, Barendregt A, Westphal AH, van Duijn E, Mattevi A, van Berkel WJ J Biol Chem. 2013 Jul 17. PMID:23864660 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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