4MH1

Crystal structure and functional studies of quinoprotein L-sorbose dehydrogenase from Ketogulonicigenium vulgare Y25

Summary for 4MH1

• Entry DOI: 10.2210/pdb4mh1/pdb
• Descriptor: Sorbose dehydrogenase, PYRROLOQUINOLINE QUINONE, CALCIUM ION (3 entities in total)
• Functional Keywords: 2-keto-l-gulonic acid, ketogulonicigenium vulgare, l-sorbose dehydrogenase, beta-propeller, hydrolase, carbohydrate/sugar binding, periplasmic, oxidoreductase
• Biological source: Ketogulonicigenium vulgare
• Total number of polymer chains: 2
• Total formula weight: 122897.10

Authors

Han, X.,Liu, X. (deposition date: 2013-08-29, release date: 2014-07-23, Last modification date: 2024-11-20)

Primary citation

Han, X.,Xiong, X.,Jiang, D.,Chen, S.,Huang, E.,Zhang, W.,Liu, X.
Crystal structure of L-sorbose dehydrogenase, a pyrroloquinoline quinone-dependent enzyme with homodimeric assembly, from Ketogulonicigenium vulgare
Biotechnol.Lett., 36:1001-1008, 2014

PubMed 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.

PubMed: 24557074
DOI: 10.1007/s10529-013-1446-5

Experimental method

X-RAY DIFFRACTION (2.7 Å)