2W37

CRYSTAL STRUCTURE OF THE HEXAMERIC CATABOLIC ORNITHINE TRANSCARBAMYLASE FROM Lactobacillus hilgardii

Summary for 2W37

• Entry DOI: 10.2210/pdb2w37/pdb
• Descriptor: ORNITHINE CARBAMOYLTRANSFERASE, CATABOLIC, NICKEL (II) ION (3 entities in total)
• Functional Keywords: transcarbamylase, metal binding-site, hexamer, cytoplasm, ornithine, transferase, arginine metabolism, carbamoyl phosphate
• Biological source: LACTOBACILLUS HILGARDII
• Cellular location: Cytoplasm (Probable): Q8G998
• Total number of polymer chains: 3
• Total formula weight: 120458.46

Authors

de las Rivas, B.,Fox, G.C.,Angulo, I.,Rodriguez, H.,Munoz, R.,Mancheno, J.M. (deposition date: 2008-11-06, release date: 2009-11-17, Last modification date: 2023-12-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)