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• W2147029554 abstract "Using synchrotron radiation, X-ray data have been collected from Pyrococcus furiosus ornithine carbamoyltransferase (Pfu OTCase) to a maximal resolution of 1.87 Å, allowing the refinement of a previous structure at 2.7 Å [Villeret et al. (1998), Proc. Natl Acad. Sci. USA, 95, 2801–2806]. Thanks to the high resolution of this refined structure, two sulfate ions and 191 water molecules could be localized directly from the electron-density maps. The identification of these molecules allowed a more rigorous description of the active site and the identification of residues involved in binding carbamoyl phosphate. The improved quality of the model resulted in a better definition of several loops and the various interfaces. The dodecameric protein is composed of four catalytic trimers disposed in a tetrahedral manner. The extreme thermal stability of Pfu OTCase is mainly the result of the strengthening of the intersubunit interactions in a trimer and oligomerization of the trimers into a dodecamer. Interfaces between monomers in a catalytic trimer are characterized by an increase in ion-pair networks compared with mesophilic OTCases. However, the interfaces between catalytic trimers in the dodecameric oligomer are mainly hydrophobic and also involve aromatic–aromatic and cation–π interactions." @default.
• W2147029554 created "2016-06-24" @default.
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• W2147029554 creator A5074695609 @default.
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• W2147029554 date "2003-11-27" @default.
• W2147029554 modified "2023-09-29" @default.
• W2147029554 title "Refined structure of<i>Pyrococcus furiosus</i>ornithine carbamoyltransferase at 1.87 A" @default.
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• W2147029554 doi "https://doi.org/10.1107/s0907444903019231" @default.
• W2147029554 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14646072" @default.
• W2147029554 hasPublicationYear "2003" @default.
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