2W37

CRYSTAL STRUCTURE OF THE HEXAMERIC CATABOLIC ORNITHINE TRANSCARBAMYLASE FROM Lactobacillus hilgardii

2W37 の概要

• エントリーDOI: 10.2210/pdb2w37/pdb
• 分子名称: ORNITHINE CARBAMOYLTRANSFERASE, CATABOLIC, NICKEL (II) ION (3 entities in total)
• 機能のキーワード: transcarbamylase, metal binding-site, hexamer, cytoplasm, ornithine, transferase, arginine metabolism, carbamoyl phosphate
• 由来する生物種: LACTOBACILLUS HILGARDII
• 細胞内の位置: Cytoplasm (Probable): Q8G998
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 120458.46

構造登録者

de las Rivas, B.,Fox, G.C.,Angulo, I.,Rodriguez, H.,Munoz, R.,Mancheno, J.M. (登録日: 2008-11-06, 公開日: 2009-11-17, 最終更新日: 2023-12-13)

主引用文献

De Las Rivas, B.,Fox, G.C.,Angulo, I.,Ripoll, M.M.,Rodriguez, H.,Munoz, R.,Mancheno, J.M.
Crystal Structure of the Hexameric Catabolic Ornithine Transcarbamylase from Lactobacillus Hilgardii: Structural Insights Into the Oligomeric Assembly and Metal Binding.
J.Mol.Biol., 393:425-, 2009

PubMed Abstract: Catabolic ornithine transcarbamylase (cOTC; EC 2.1.3.3) catalyzes the formation of ornithine (ORN) and carbamoyl phosphate from citrulline, which constitutes the second step of the degradation of arginine via the arginine deiminase pathway. Here, we report the crystal structure of cOTC from the lactic acid bacteria Lactobacillus hilgardii (Lh-cOTC) refined to 2.1 A resolution. The structure reveals that Lh-cOTC forms a hexameric assembly, which was also confirmed by gel-filtration chromatography and analytical ultracentrifugation. The homohexamer, with 32 point group symmetry, represents a new oligomeric state within the members of the ornithine transcarbamylase family that are typically homotrimeric or homododecameric. The C-terminal end from each subunit constitutes a key structural element for the stabilization of the hexameric assembly in solution. Additionally, the structure reveals, for the first time in the ornithine transcarbamylase family, a metal-binding site located at the 3-fold molecular symmetry axis of each trimer.

PubMed: 19666033
DOI: 10.1016/J.JMB.2009.08.002

実験手法

X-RAY DIFFRACTION (2.1 Å)