1PVV

Refined Structure of Pyrococcus furiosus Ornithine Carbamoyltransferase at 1.87 A

1PVV の概要

• エントリーDOI: 10.2210/pdb1pvv/pdb
• 関連するPDBエントリー: 1a1s
• 分子名称: Ornithine carbamoyltransferase, SULFATE ION (3 entities in total)
• 機能のキーワード: dodecamer, transferase
• 由来する生物種: Pyrococcus furiosus
• 細胞内の位置: Cytoplasm: Q51742
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35421.51

構造登録者

Massant, J.,Wouters, J.,Glansdorff, N. (登録日: 2003-06-29, 公開日: 2003-12-09, 最終更新日: 2023-08-16)

主引用文献

Massant, J.,Wouters, J.,Glansdorff, N.
Refined structure of Pyrococcus furiosus ornithine carbamoyltransferase at 1.87 A.
Acta Crystallogr.,Sect.D, 59:2140-2149, 2003

PubMed Abstract: Using synchrotron radiation, X-ray data have been collected from Pyrococcus furiosus ornithine carbamoyltransferase (Pfu OTCase) to a maximal resolution of 1.87 A, allowing the refinement of a previous structure at 2.7 A [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-pi interactions.

PubMed: 14646072
DOI: 10.1107/S0907444903019231

実験手法

X-RAY DIFFRACTION (1.87 Å)