Structural highlights
Publication Abstract from PubMed
The crystal structure of the L-sorbose dehydrogenase (SDH) from Ketogulonicigenium vulgare Y25 has been determined at 2.7 A resolution using the molecular replacement method. The overall structure of SDH is similar to that of other quinoprotein dehydrogenases; consisting of an eight bladed beta-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.
Crystal structure of L-sorbose dehydrogenase, a pyrroloquinoline quinone-dependent enzyme with homodimeric assembly, from Ketogulonicigenium vulgare.,Han X, Xiong X, Jiang D, Chen S, Huang E, Zhang W, Liu X Biotechnol Lett. 2014 May;36(5):1001-8. doi: 10.1007/s10529-013-1446-5. Epub 2014, Feb 21. PMID:24557074[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2014 May;36(5):1001-8. doi: 10.1007/s10529-013-1446-5. Epub 2014, Feb 21. PMID:24557074 doi:http://dx.doi.org/10.1007/s10529-013-1446-5
