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2.1.3.3: ornithine carbamoyltransferase

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

Word Map on EC 2.1.3.3

Reaction

Carbamoyl phosphate
+
L-ornithine
=
phosphate
 +
L-citrulline

Synonyms

anabolic ornithine carbamoyltransferase, anabolic ornithine transcarbamoylase, AOTC, arcB gene product, ArgF, ArgK, aTtOTCase, carbamoyltransferase, carbamoyltransferase, ornithine, carbamylphosphate-ornithine transcarbamylase, catabolic ornithine carbamoyltransferase, catabolic ornithine transcarbamylase, citrulline phosphorylase, cOTC, L-ornithine carbamoyltransferase, L-ornithine carbamyltransferase, L-ornithine transcarbamylase, Lmo0036, MB1684, Mtb OTC, OCT, ornithine carbamoyltransferase, ornithine carbamoytransferase, ornithine carbamyl transferase, ornithine carbamyltransferase, ornithine transcarbamoylase, ornithine transcarbamylase, ornithine transcarbamylase 3, OTC, otcase, ROTCase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.3 Carboxy- and carbamoyltransferases
                2.1.3.3 ornithine carbamoyltransferase

Crystallization

Crystallization on EC 2.1.3.3 - ornithine carbamoyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
unliganded aOTC, hanging drop vapor diffusion method, mixing of 500 nl 10 mg/ml protein solution with 500 nl well solution containing 25% PEG 3350, 0.2 M NaCl, 0.1 M HEPES, pH 8.0, room temperature, 1 week, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement and modeling
purified full-length enzyme or in complex with inhibitors N-(phosphonoacetyl)-putrescine or N-(phosphonoacetyl)-L-ornithine, and trunacted enzyme in complex with N-(phosphonoacetyl)-L-ornithine, hanging drop vapor diffusion technique, mixing of 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5 containing 0.43 mM ligand with 0.001 ml of crystallization solution composed of 125 mM (NH4)2SO4, 17% PEG 3350, 0.1 M Bis-Tris, pH 5.5, 21°C, X-ray diffraction structure determination and analysis at 2.5 A, 2.0 A, and 1.59 A resolution, respectively, modeling
ornithine carbamoyltransferase-Ndelta-(N'-sulfodiaminophosphinyl)-L-ornithine complex, hanging-drop vapour diffusion, equal volumes of protein are combined with a solution containing 17.8% polyethylene glycol 8000 and 2.2% polyethylene glycol 1000, pyramidal crystals after 1-2 weeks
one protein molecule per asymmetric unit, trimeric structure
-
complexed with the bisubstrate analog N-phosphoacetyl-L-ornithine
-
ornithine transcarbamoylase-carbamoylphosphate complex, X-ray structure at 2.4-2.6 A resolution
hanging drop vapor diffusion method
-
to 2.1 A resolution. enzyme forms a homohexamer with 32 point group symmetry. The C-terminal end from each subunit constitutes a key structural element for the stabilization of the hexameric assembly in solution
hanging drop vapor diffusion method, crystal structures of Mtb OTC in orthorhombic and hexagonal form hexagonal form crystals complexed with carbamoyl phosphate and L-norvaline
crystal structure determination of the E105G mutant at 3.0 A resolution
-
T allosteric form, hanging-drop vapour diffusion against a reservoir solution containing 100 mM glycylglycin, pH 9, 12% polyethylene glycol 6000 and 1 mM dithiothreitol, X-ray analysis, 4.5 A resolution, R allosteric form, hanging-drop vapour diffusion against a reservoir solution containing 1.9 M ammonium sulfate, 50 mM HEPES, pH 7.2, 1 mM DTT, 1 mM EDTA, 3% polyethylene glycol 400 and 10 mM spermidine
-
dodecamer, four catalytic trimers disposed in a tetrahedral manner
-
hanging-drop vapor diffusion, 1/1 mixture of 12 mg/ml enzyme solution and a reservoir solution containing 1 M NaCl, 100 mM acetate buffer, pH 4.0, crystals are obtained after 7-10 days, X-ray structure at 2.7 A resolution
-
purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of protein in 20 mM Tris-HCl, pH 8.0, and 200 mM NaCl, with 0.001 ml of well solution containing 10% PEG 4000, 0.1 M NaCl, 0.1 M HEPES-Na, pH 7.5, 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution, modeling