Purification, crystallization and preliminary X-ray analysis of catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa.
The catabolic ornithine carbamoyltransferase (OTCase) from Pseudomonas aeruginosa exhibits allosteric behaviour, with two conformational states of the molecule: an active R form and an inactive T form. The enzyme is a dodecamer with a molecular mass of 455700 Da. Three crystal forms have been obtained. Crystals of allosteric state T are rhombohedral, belonging to the R3 space group, with hexagonal unit-cell parameters a = b = 180.6, c = 122.0 A. They diffract to a resolution of 4.5 A. Two crystal forms for allosteric state R have been obtained, with hexagonal and cubic symmetries. Hexagonal crystals, which diffract to a resolution of 3. 4 A, belong to the space group P6(3) with unit-cell parameters a = b = 140.8, c = 145.6 A. The cubic crystals belong to space group I23, with unit-cell parameter a = 134.32 A and diffract to a resolution better than 2.5 A. In all crystal forms, the dodecamer exhibits a 23 point-group symmetry.
Sainz
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Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale J.-P. Ebel (CEA-CNRS), 41 Rue Jules Horowitz, F-38027 Grenoble CEDEX 1, France.
Vicat
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J
Kahn
R
R
Tricot
C
C
Stalon
V
V
Dideberg
O
O
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D002384:Catalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D009954:Ornithine Carbamoyltransferase / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D001426:Bacterial Proteins; D009954:Ornithine Carbamoyltransferase