1dxh
From Proteopedia
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| , resolution 2.50Å | |||||||
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| Ligands: | |||||||
| Activity: | Ornithine carbamoyltransferase, with EC number 2.1.3.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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