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2.7.7.9: UTP-glucose-1-phosphate uridylyltransferase

This is an abbreviated version!
For detailed information about UTP-glucose-1-phosphate uridylyltransferase, go to the full flat file.

Word Map on EC 2.7.7.9

Reaction

UTP
+
alpha-D-glucose 1-phosphate
=
diphosphate
 +
UDP-glucose

Synonyms

All3274, CugP, cyanobacterial UDP-Glc PPase, ExoN, GalU, gfugp, Glc-1-P UTase, GlcNAc-1-P UTase, glucose 1-phosphate uridylyltransferase, glucose-1-phosphate urididyltransferase, glucose-1-phosphate uridyltransferase, glucose-1-phosphate uridylyltransferase, KF278717, plastid UDP-glucose pyrophosphorylase, rml-1, ScUGPase-1, sll1558, ST0452, ST0452 protein, STK_04520, sugar-1-P NTase, sugar-1-phosphate nucleotidylyltransferase, TaGalU, UDP glucose pyrophosphorylase, UDP-Glc pyrophosphorylase, UDP-GlcPPase, UDP-glucose pyrophosphorylase, UDP-glucose pyrophosphorylase 1, UDP-glucose pyrophosphorylase isoenzyme UGP5, UDP-glucose pyrophosphorylase UGP1, UDP-glucose pyrophosphorylase UGP2, UDP-glucose pyrophosphorylase UGP3, UDPG phosphorylase, UDPG pyrophosphorylase, UDPG-pyrophosphorylase, UDPglucose pyrophosphorylase, UDPGP, UGP, ugp-1, UGP1, UGP3, UgpA, UGPase, UGPase1, UGPase2, UGPG-PPase, UPD1, uridine 5'-diphosphoglucose pyrophosphorylase, uridine diphosphate-D-glucose pyrophosphorylase, uridine diphosphate-glucose pyrophosphorylase, uridine diphosphoglucose pyrophosphorylase, uridine-diphosphate glucose pyrophosphorylase, uridylyltransferase, glucose 1-phosphate, UTP/dTTP-glucose-1-phosphate uridylyl/thymidylyl transferase, UTP:alpha-D-glucose uridylyltransferase, UTP:glucose-1-phosphate uridylyltransferase, VldB

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.9 UTP-glucose-1-phosphate uridylyltransferase

Crystallization

Crystallization on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
uncomplexed enzyme and in presence of UTP and UDP-glucose. Structures show a carboxy-terminal beta-helix domain in a unique orientation. The nucleotide binding loop and the carboxy-terminal domain, including the possible catalytically important K360, move in and out of the active site in a concerted fashion
from ammonium sulfate precipitate
in complex with both Mg2+ and UDP-glucose. Residues involved in anchoring the ligand to the active site include the polypeptide chain backbone atoms of Ala20, Gly21, Gly117, Gly180, and Ala214, and the side chains of Glu36, Gln112, Asp143, Glu201, and Lys202. Two magnesium ions are coordinated to the UDP-glucose. An alpha- and a beta-phosphoryl oxygen, three waters, and the side chain of Asp142 ligate the first Mg2+ ion, whereas the second ion is coordinated by an alpha-phosphoryl oxygen and five waters
-
in presence of both magnesium and UDP-glucose. Residues anchoring the ligand to the acitve site include polypepetide backbone atoms of A20, G21, G117, G180 and A214 and side chain residues of E36, Q112, D143, E201, and K202. Two magnesium ions coordinate to UDP-glucose
-
protein is a tetramer with 222 point group symmetry. Each subunit is dominated by an eight-stranded mixed beta-sheet with two additional layers of beta-sheets and ten alpha-helices. Q109 and D137 anchor the uracil ring and the ribose of UDP-glucose to the protein.The beta-phosphoryl group of the product lies close to the epsilon-nitrogen of K202, the carboxylate group of E201 can bridge the 2’- and 3’-hydroxyl groups of the glucosyl moiety
to 1.9 A resolution. Modeling of UDP-glucose into the active site. The side chains of Gln109 and Asp137, respectively, serve to anchor the uracil ring and the ribose of UDP-glucose to the protein. The beta-phosphoryl group of the product is predicted to lie within hydrogen bonding distance to the eosilon-nitrogen of Lys202 whereas the carboxylate group of Glu201 is predicted to bridge the 2'- and 3'-hydroxyl groups of the glucosyl moiety
apo- and UDP-glucose/Mg2+-bound enzyme complexes, hanging drop and sitting drop vapor diffusion methods, protein in 20 mM Tris-HCl pH 7.5 and 0.1 M NaCl, is mixed with 0.1 M sodium acetate trihydrate, pH 4.6, 2 M ammonium sulfate and 0.1 M guanidine-HCl for the apo-enzyme crystals, 22°C, one week. UDP-Glc/Mg2+-bound holo-UGPase is crystallized in 0.1 M HEPES-Na, pH 7.5, 2% PEG 400 and 1.5 M ammonium sulfate containing 10 mM UDP-Glc and 10 mM MgCl2 at 22°C within a month, X-ray diffraction structure determination and analysis at 2.9 A and 2.3 A resolutions, respectively
in the D4 octameric structure of the hUGP1-UDP-Glc complex, all subunits have the same overall conformation. The transition of the UGP octamer between the apo- and the product-bound forms is in agreement with the Monod-Wyman-Changeux symmetry model. oligomerzation facilitates an intermolecular stabilization of the sugar moiety in the active site (interlock mechanism), enhances protein stability, enables mild positive cooperativity observed for the octameric wild-type UGP1 towards diphosphate in the reverse reaction, and may allow regulation of the UGP octamer by modification of a single subunit
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 20 mM Tris/HCl, pH 8.0, and 200 mM NaCl, with 0.001 ml of reservoir solution containing 100 mM HEPES, pH 6.5, 5 mM MgSO4, 15% w/v PEG 3350 and 20% v/v glycerol, 20°C, X-ray diffraction structure determination and analysis at 3.6 A resolution, molecular replacement
uncomplexed apo-protein with open conformation and in complex with UDP-glucose and closed conformation. the central catalyitc domain resembles a Rossman fold and contains key residues. The C-terminal domain forms a left-handed parallel beta-helix
-
from ammonium sulfate precipitate
both in solution and crystal, enzyme forms homooctamers. Association of octamers is mediated by left-handed helices in the C-terminal domains forming a toroidal solenoid structure. The catalytic domains do not directly contact each other, consistent with simple Michaelis-Menten kinetics
-
hanging-drop vapour-diffusion method at 20°C, crystal structure at resolution of 2.0 A. The crystals reveals the presence of two molecules in the asymmetric unit
detailed comparison between enzyme and thymidylyltransferases
-
in complex with glucose 1-phosphate, data from an osmium derivative and a selenomethiomine derivative
-
native and seleno-methionine-derivatized proteins, in complex with glucose 1-phosphate, to 2.65 A resolution. Detailed comparison with thymidylyltransferases
-
purified recombinant enzyme, 17 mg/mL protein is mixed 1:1 with a crystallization buffer of 22% PEG 3350, 0.1 M ammonium sulfate, and 0.1 M Bis-Tris, pH 5.5, X-ray diffraction structure determination and analysis at 1.92 A resolution