2hk1
From Proteopedia
(New page: 200px<br /><applet load="2hk1" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hk1, resolution 2.300Å" /> '''Crystal structure o...) |
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==Overview== | ==Overview== | ||
| - | D-psicose, a rare sugar produced by the enzymatic reaction of D-tagatose | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Agrobacterium tumefaciens]] | [[Category: Agrobacterium tumefaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cha, S | + | [[Category: Cha, S S.]] |
| - | [[Category: Kim, H | + | [[Category: Kim, H J.]] |
[[Category: Kim, K.]] | [[Category: Kim, K.]] | ||
| - | [[Category: Oh, D | + | [[Category: Oh, D K.]] |
[[Category: Rhee, S.]] | [[Category: Rhee, S.]] | ||
[[Category: FRU]] | [[Category: FRU]] | ||
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[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:40 2008'' |
Revision as of 15:42, 21 February 2008
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Crystal structure of D-psicose 3-epimerase (DPEase) in the presence of D-fructose
Overview
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.
About this Structure
2HK1 is a Single protein structure of sequence from Agrobacterium tumefaciens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of D-psicose 3-epimerase from Agrobacterium tumefaciens and its complex with true substrate D-fructose: a pivotal role of metal in catalysis, an active site for the non-phosphorylated substrate, and its conformational changes., Kim K, Kim HJ, Oh DK, Cha SS, Rhee S, J Mol Biol. 2006 Sep 1;361(5):920-31. Epub 2006 Jul 28. PMID:16876192
Page seeded by OCA on Thu Feb 21 17:42:40 2008
Categories: Agrobacterium tumefaciens | Single protein | Cha, S S. | Kim, H J. | Kim, K. | Oh, D K. | Rhee, S. | FRU | MN | Tim-barrel
