1dxh
From Proteopedia
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CATABOLIC ORNITHINE CARBAMOYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA
Overview
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.
About this Structure
1DXH is a Single protein structure of sequence from Pseudomonas aeruginosa with as ligand. Active as Ornithine carbamoyltransferase, with EC number 2.1.3.3 Full crystallographic information is available from OCA.
Reference
Purification, crystallization and preliminary X-ray analysis of catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa., Sainz G, Vicat J, Kahn R, Tricot C, Stalon V, Dideberg O, Acta Crystallogr D Biol Crystallogr. 1999 Sep;55(Pt 9):1591-3. PMID:10489456
Page seeded by OCA on Thu Feb 21 12:21:32 2008
