title: Crystal structure of L-sorbose dehydrogenase, a pyrroloquinoline quinone-dependent enzyme with homodimeric assembly, from Ketogulonicigenium vulgare.
abstract: The crystal structure of the L-sorbose dehydrogenase (SDH) from Ketogulonicigenium vulgare Y25 has been determined at 2.7 Å resolution using the molecular replacement method. The overall structure of SDH is similar to that of other quinoprotein dehydrogenases; consisting of an eight bladed β-propeller PQQ domain and protrusion loops. We identified a stable homodimer in crystal and demonstrated its existence in solution by sedimentation velocity measurement. By biochemical characterization of the SDH in vitro, using L-sorbose as substrate and cytochrome c551 as electron acceptor, we revealed cytochrome c551 acting as physiological primary electron acceptor for SDH.
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin, 300071, China, hxdon@126.com.
authors.forename: Xiaodong
authors.initials: X
authors.lastname: Han
authors.forename: Xianghua
authors.initials: X
authors.lastname: Xiong
authors.forename: Dunquan
authors.initials: D
authors.lastname: Jiang
authors.forename: Sihan
authors.initials: S
authors.lastname: Chen
authors.forename: Enyu
authors.initials: E
authors.lastname: Huang
authors.forename: Weicai
authors.initials: W
authors.lastname: Zhang
authors.forename: Xinqi
authors.initials: X
authors.lastname: Liu
mesh_terms: D000595:Amino Acid Sequence; D002118:Calcium / Q000737:chemistry / Q000378:metabolism; D002237:Carbohydrate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D045542:PQQ Cofactor / Q000737:chemistry* / Q000378:metabolism; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D041902:Rhodobacteraceae / Q000201:enzymology*; D016415:Sequence Alignment
chemical_list: D021122:Protein Subunits; D045542:PQQ Cofactor; D002237:Carbohydrate Dehydrogenases; C104557:sorbose dehydrogenase; D002118:Calcium