2hk0: Difference between revisions

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[[Image:2hk0.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_2hk0|  PDB=2hk0  |  SCENE=  }}  
{{STRUCTURE_2hk0|  PDB=2hk0  |  SCENE=  }}  


'''Crystal structure of D-psicose 3-epimerase (DPEase) in the absence of substrate'''
===Crystal structure of D-psicose 3-epimerase (DPEase) in the absence of substrate===




==Overview==
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D-psicose, a rare sugar produced by the enzymatic reaction of D-tagatose 3-epimerase (DTEase), has been used extensively for the bioproduction of various rare carbohydrates. Recently characterized D-psicose 3-epimerase (DPEase) from Agrobacterium tumefaciens was found to belong to the DTEase family and to catalyze the interconversion of D-fructose and D-psicose by epimerizing the C-3 position, with marked efficiency for D-psicose. The crystal structures of DPEase and its complex with the true substrate D-fructose were determined; DPEase is a tetramer and each monomer belongs to a TIM-barrel fold. The active site in each subunit is distinct from that of other TIM-barrel enzymes, which use phosphorylated ligands as the substrate. It contains a metal ion with octahedral coordination to two water molecules and four residues that are absolutely conserved across the DTEase family. Upon binding of D-fructose, the substrate displaces water molecules in the active site, with a conformation mimicking the intermediate cis-enediolate. Subsequently, Trp112 and Pro113 in the beta4-alpha4 loop undergo significant structural changes, sealing off the active site. Structural evidence and site-directed mutagenesis of the putative catalytic residues suggest that the metal ion plays a pivotal role in catalysis by anchoring the bound D-fructose, and Glu150 and Glu244 carry out an epimerization reaction at the C-3 position.
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{{ABSTRACT_PUBMED_16876192}}


==About this Structure==
==About this Structure==
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[[Category: Rhee, S.]]
[[Category: Rhee, S.]]
[[Category: Tim-barrel]]
[[Category: Tim-barrel]]
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