1kdg

Crystal structure of the flavin domain of cellobiose dehydrogenase

spinqualitylabelsall models 1kdg, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1kdg is a 2 chain structure with sequence from Phanerochaete chrysosporium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 6FA, EMT, HG, MAN, NAG, UNX Related: 1d7b, 1d7c, 1d7d Activity: Oxidoreductase, with EC number 1.1.99.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CDH_PHACH] Degrades both lignin and cellulose. Oxidizes cellobiose to cellobionolactone. 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 Cellobiose dehydrogenase (CDH) participates in the degradation of cellulose and lignin. The protein is an extracellular flavocytochrome with a b-type cytochrome domain (CYT(cdh)) connected to a flavodehydrogenase domain (DH(cdh)). DH(cdh) catalyses a two-electron oxidation at the anomeric C1 position of cellobiose to yield cellobiono-1,5-lactone, and the electrons are subsequently transferred from DH(cdh) to an acceptor, either directly or via CYT(cdh). Here, we describe the crystal structure of Phanerochaete chrysosporium DH(cdh) determined at 1.5 A resolution. DH(cdh) belongs to the GMC family of oxidoreductases, which includes glucose oxidase (GOX) and cholesterol oxidase (COX); however, the sequence identity with members of the family is low. The overall fold of DH(cdh) is p-hydroxybenzoate hydroxylase-like and is similar to, but also different from, that of GOX and COX. It is partitioned into an FAD-binding subdomain of alpha/beta type and a substrate-binding subdomain consisting of a seven-stranded beta sheet and six helices. Docking of CYT(cdh) and DH(cdh) suggests that CYT(cdh) covers the active-site entrance in DH(cdh), and that the resulting distance between the cofactors is within acceptable limits for inter-domain electron transfer. Based on docking of the substrate, cellobiose, in the active site of DH(cdh), we propose that the enzyme discriminates against glucose by favouring interaction with the non-reducing end of cellobiose. Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase.,Hallberg BM, Henriksson G, Pettersson G, Divne C J Mol Biol. 2002 Jan 18;315(3):421-34. PMID:11786022 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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