1KDG

Crystal structure of the flavin domain of cellobiose dehydrogenase

Summary for 1KDG

• Entry DOI: 10.2210/pdb1kdg/pdb
• Related: 1D7B 1D7C 1D7D
• Descriptor: cellobiose dehydrogenase, 2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (8 entities in total)
• Functional Keywords: gmc oxidoreductase, phbh fold, alpha/beta structure, rossmann fold, 6-hydroxylated fad, oxidoreductase
• Biological source: Phanerochaete chrysosporium
• Cellular location: Secreted: Q01738
• Total number of polymer chains: 2
• Total formula weight: 121618.85

Authors

Hallberg, B.M.,Henriksson, G.,Pettersson, G.,Divne, C. (deposition date: 2001-11-13, release date: 2002-11-13, Last modification date: 2024-10-16)

Primary citation

Hallberg, B.M.,Henriksson, G.,Pettersson, G.,Divne, C.
Crystal Structure of the Flavoprotein Domain of the Extracellular Flavocytochrome Cellobiose Dehydrogenase
J.Mol.Biol., 315:421-434, 2002

PubMed Abstract: 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.

PubMed: 11786022
DOI: 10.1006/jmbi.2001.5246

Experimental method

X-RAY DIFFRACTION (1.5 Å)