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 obtain...
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Published in | Acta crystallographica. Section D, Biological crystallography. Vol. 55; no. 9; pp. 1591 - 1593 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
5 Abbey Square, Chester, Cheshire CH1 2HU, England
International Union of Crystallography
01.09.1999
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Subjects | |
Online Access | Get full text |
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Summary: | 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 Å. They diffract to a resolution of 4.5 Å. 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 Å, belong to the space group P63 with unit‐cell parameters a = b = 140.8, c = 145.6 Å. The cubic crystals belong to space group I23, with unit‐cell parameter a = 134.32 Å and diffract to a resolution better than 2.5 Å. In all crystal forms, the dodecamer exhibits a 23 point‐group symmetry. |
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Bibliography: | ark:/67375/WNG-Q8BT3TV3-1 ArticleID:AYDLI0341 istex:BEE456EE084F355B77D3B9D7E14D819DC368516D ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1399-0047 0907-4449 1399-0047 |
DOI: | 10.1107/S0907444999007970 |