3vnm | pdb_00003vnm

Crystal structures of D-Psicose 3-epimerase with D-sorbose from Clostridium cellulolyticum H10

spinqualitylabelsall models 3vnm, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vnm is a 4 chain structure with sequence from Ruminiclostridium cellulolyticum H10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.12Å Ligands: MN, SDD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DPES_RUMCH Involved in the biosynthesis of D-psicose. Catalyzes the reversible epimerization of D-fructose at the C3 position to yield D-psicose. The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose. Publication Abstract from PubMed D-psicose 3-epimerase (DPEase) is demonstrated to be useful in the bioproduction of D-psicose, a rare hexose sugar, from D-fructose, found plenty in nature. Clostridium cellulolyticum H10 has recently been identified as a DPEase that can epimerize D-fructose to yield D-psicose with a much higher conversion rate when compared with the conventionally used DTEase. In this study, the crystal structure of the C. cellulolyticum DPEase was determined. The enzyme assembles into a tetramer and each subunit shows a (beta/alpha)(8) TIM barrel fold with a Mn(2+) metal ion in the active site. Additional crystal structures of the enzyme in complex with substrates/products (D-psicose, D-fructose, D-tagatose and D-sorbose) were also determined. From the complex structures of C. cellulolyticum DPEase with D-psicose and D-fructose, the enzyme has much more interactions with D-psicose than D-fructose by forming more hydrogen bonds between the substrate and the active site residues. Accordingly, based on these ketohexose-bound complex structures, a C3-O3 proton-exchange mechanism for the conversion between D-psicose and D-fructose is proposed here. These results provide a clear idea for the deprotonation/protonation roles of E150 and E244 in catalysis. Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars.,Chan HC, Zhu Y, Hu Y, Ko TP, Huang CH, Ren F, Chen CC, Ma Y, Guo RT, Sun Y Protein Cell. 2012 Feb;3(2):123-31. Epub 2012 Mar 17. PMID:22426981 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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