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2.5.1.17: corrinoid adenosyltransferase

This is an abbreviated version!
For detailed information about corrinoid adenosyltransferase, go to the full flat file.

Word Map on EC 2.5.1.17

Reaction

2 ATP + 2 cob(II)alamin +

a reduced flavoprotein
= 2 triphosphate + 2 adenosylcob(III)alamin +
an oxidized flavoprotein

Synonyms

ACAT, adenosyltransferase, vitamin B12s, aquacob(I)alamin adenosyltransferase, aquocob(I)alamin adenosyltransferase, ATP: cobalamin adenosyltransferase, ATP:co(I)rrinoid adenosyltransferase, ATP:cob(I)alamin adenosyltransferase, ATP:cob(I)alamin Cobeta-adenosyltransferase, ATP:cob(I)alamin transferase (ATR), ATP:Cob(I)alaminadenosyltransferase, ATP:cobalamin adenosyltransferase, ATP:cobalt(I) corrinoid adenosyltransferase, ATP:corrinoid adenosyltransferase, ATP:corrinoid adenosyltransferase PduO, ATR, cob(I)alamin adenosyltransferase, cob(I)yrinic acid a,c-diamide adenosyltransferase, CobA, CobA-type ATP:Co(I)rrinoid adenosyltransferase, cobalamin adenosyltransferase, CobAMm, cobO mutant SVQ336, cobO mutant SVQ524, cobO mutantSVQ336, EC 1.16.8.1, EutT, EutT adenosyltransferase, hATR, homologeous to PduO-type ATP: cob(I)alamin adenosyltransferase, human adenosyltransferase, human ATP: cob(I)alamin adenosyltransferase, human-type ACA, human-type ATP: co(I)rrinoid adenosyltransferase, human-type ATP: cob(I)alamin adenosyltransferase, LrPduO, methylmalonic aciduria type B, MMAB, MMAB protein, PduO, PduO adenosyltransferase, PduO enzyme, PduO protein, PduO-type ACA, PduO-type adenosine 5'-triphosphate:corrinoid adenosyltransferase, PduO-type ATP: cobalamin adenosyltransferase, PduO-type ATP:Co(I)rrinoid adenosyltransferase, PduO-type ATP:cob(I)alamin adenosyltransferase, PduO-type ATP:corrinoid adenosyltransferase, PduO-type corrinoid adenosyltransferase, ST1454, ST2180, TA1434, vitamin B12s adenosyltransferase

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.17 corrinoid adenosyltransferase

Crystallization

Crystallization on EC 2.5.1.17 - corrinoid adenosyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and in complex with Mg2+/ATP, C-centred orthorhombic space group C222(1), unit cell parameters: a: 64.93 A, b: 137.08 A, c: 158.55 A, alpha, beta, gamma: 90°, one trimer in the asymmetric unit, sitting-drop combined with hanging-drop vapour-diffusion method: 13 mg/ml protein solution, precipitants: 1.55-1.6 M ammonium sulfate, 9-10% (v/v) dioxane (pH 6.5), for complex: 4 mM ATP and 4 mM Mg2+
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purified recombinant PduO in complex with ATP, hanging drop vapor diffusion method, mixing o 0.001 ml of 13 mg/ml protein solution, with or without 4 mM ATP and 4 mM MgCl2, with 0.001 ml of optimized reservoir solution containing 100 mM MES, pH 6.5, 1.52 M ammonium sulfate, 9% v/v dioxane, followed by equilibration over 0.5 ml of the mother liquor, the cryoprotection solution contains 50 mM MES, pH 6.5, 0.76 M ammonium sulfate, 4.5% v/v dioxane, and 1.7 M sodium malonate, pH 7.0, X-ray diffraction structure determination and analysis
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native (PDB: 2ZHY, with ordered N-terminal loop and formed active site) and in complex with ATP (PDB: 2ZHZ, substrate-binding cleft is widened and the N-terminal loop swung out and conformational shift of Arg129 side chain upon ATP-binding, similar structure to human and Lactobacillus reuteri PduO except for interaction of NH2 nitrogen atom of Arg11 with gamma-phosphate of ATP), five alpha helix bundle, monomeric subunits almost identical conformations in both structures, crystals: orthothrombic space group C222(1), three monomers in the asymmetric unit, unit cell parameters: a: 52.55/53.91, b: 148.98/148.17, c: 157.35/158.10, microcrystals (from sitting-drop vapour-diffusion at 22°C) scaled up by hanging-drop vapour diffusion, reservoir solution (pH5.7, 22% (w/v) isopropanol, 12% (v/v) PEG4000), PduO-MgATP complex: ATP soaked into native PduO crystals, molecular replacement using PDB: 2G2D as model
mutants D35N (without tag) in complex with ATP and cob(II)alamin and R132K (without tag) in complex with ATP, thin plate crystals, space group P6(3), two monomers in the asymmetric unit, unit cell parameters: a, b: 65A, c: 169A, beta: 90°; vapour-diffusion under anoxic conditions, protein solution (15 mg/ml, containing ATP, hydroxycobalamin and a reducing system of NADH, FMN, and flavodoxin reductase), reservoir solution (incl. 14-16% PEG8000, pH6)
-
purified recombinant His-tagged enzyme in complex with its substrates, hanging drop vapour diffusion method, 20°C, 0.004 ml of 20 mg/ml protein in 10 mM Tris-HCl, pH 8.0, is mixed with 0.004 ml od precipitant solution containing 0.1 M HEPES, pH 8.5, 1.1 M ammonium sulfate, 2 mM ATP, 55 mM MgCl2, 165 mM NaCl, and 15 mM cob(I)alamin, 7 days, X-ray diffraction structure determination and analysis at 1.68 A resolution
-
trimer of three independent five-helix bundles, active sites at the interface between adjacent monomers, no significant structural changes accompany catalysis, precatalytic complex with ATP: cob(II)alamin (PDB: 3CI1, four-coordinate, base-off cob(II)alamin intermediate, enzyme with fully ordered six C-terminal residues and potassium ion in active site), complex with tripolyphosphate: adenosylcobalamin (PDB: 3CI3, partially occupied with five-coordinate adenosylcobalamin), precatalytic complex with ATP: cob(II)inamide (PDB: 3CI4, cob(II)inamide-binding structurally indistinguishable from cob(II)alamin-binding), binding of cobalamin and cobinamide (lacking dimethylbenzimidazole moiety) in identical positions and orientation, space group R3, one molecule in asymmetric unit, unit cell parameters: a: 67.8-68, b: 67.8-68, c: 110.9-111.3, beta: 90°, molecular replacement using PDB: 2NT8 as model; vapour-diffusion with tag-cleaved protein solution (18-22 mg/ml, in presence of hydroxycobalamin and/or adenosylcobalamin or dicyanocobinamide, ATP etc.) and reservoir solution (10-13% (w/v) PEG 8000, pH 6), cubic crystals, crystallisation under anoxic conditions in presence of flavin-dependent reducing system
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purified recombinant CobA in complex with ATP, four-coordinate cobalamin, and five-coordinate cobalamin, hanging drop vapour diffusion method, 0.002 ml of 10 mg/ml CobA protein in 20 mM Tris-HCl, pH 8.0, 20 mM NADH, 3 mM ATP, 4.5 mM MgCl2, and 2 mM HOCbl, is mixed with 0.002 ml of well solution containing 100 mM MES, pH 6.0, 320 mM NaCl, and 19.6% w/v PEG4000, X-ray diffraction structure determination and analysis at 1.95 A resolution
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sitting drop vapour diffusion method. The structure of PduOC co-crystallized with heme is solved (1.9 A resolution) showing an octameric assembly with four heme moieities
3fold symmetric trimer of five counterclockwise helix bundles, one molecule in asymmetric unit, polypropylene glycol 400 molecule captured in putative active site (positively charged, important residues: Asp32, Arg118), crystals of selenomethionine derivative: space group P2(1)3, unit cell parameters: a, b, c: 84.67 A, hanging-drop vapour-diffusion method: protein solution (15 mg/ml) + reservoir solution (pH 8.1, 2.5 M ammonium sulphate, 2% polypropylene glycol 400)
hanging-drop vapor diffusion method
sparse matrix method at 20°C
trimer with noncrystallographic 3fold symmetry in the asymmetric unit, consistent of five helix bundles, identical topology to ST1454 but less ion pairs around the putative active site, crystals: space group P4(1)2(1)2, unit cell parameters: a, b: 117.58 A, c: 79.05 A, hanging-drop vapour-diffusion method: protein solution (21 mg/ml) + reservoir solution (pH6.8, 0.5 M ammonium sulfate, 2% polypropylene glycol 400), molecular replacement
purified recombinant wild-type and selenomethionine-labeled enzymes, crystal growth from 0.4 M ammonium phosphate, 4% methyl-pentanediol, 5% glycerol, at 20°C, X-ray diffraction structure determination and analysis at 1.5-1.9 A resolution