5g4l

Phloroglucinol reductase from Clostridium sp. with bound NADPH

spinqualitylabelsall models 5g4l, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g4l is a 2 chain structure with sequence from Clostridium sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Phloroglucinol reductases (PGRs) are involved in anaerobic degradation in bacteria, in which they catalyze the dearomatization of phloroglucinol into dihydrophloroglucinol. We identified three PGRs, from different bacterial species, that are members of the family of NAD(P)H-dependent short-chain dehydrogenases/reductases (SDRs). In addition to catalyzing the reduction of the physiological substrate, the three enzymes exhibit activity towards 2,4,6-trihydroxybenzaldehyde, 2,4,6-trihydroxyacetophenone, and methyl 2,4,6-trihydroxybenzoate. Structural elucidation of PGRcl and comparison to known SDRs revealed a high degree of conservation. Several amino acid positions were identified as being conserved within the PGR subfamily and might be involved in substrate differentiation. The results enable the enzymatic dearomatization of monoaromatic phenol derivatives and provide insight into the functional diversity that may be found in families of enzymes displaying a high degree of structural homology. Biocatalytic Properties and Structural Analysis of Phloroglucinol Reductases.,Conradt D, Hermann B, Gerhardt S, Einsle O, Muller M Angew Chem Int Ed Engl. 2016 Dec 12;55(50):15531-15534. doi:, 10.1002/anie.201607494. Epub 2016 Nov 22. PMID:27874239 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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