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Literature summary for 2.1.3.3 extracted from

  • 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 (2009), J. Mol. Biol., 393, 425-434.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
to 2.1 A resolution. enzyme forms a homohexamer with 32 point group symmetry. The C-terminal end from each subunit constitutes a key structural element for the stabilization of the hexameric assembly in solution Lentilactobacillus hilgardii

Metals/Ions

Metals/Ions Comment Organism Structure
additional information structure reveals a metal-binding site located at the 3fold molecular symmetry axis of each trimer within the hexamer Lentilactobacillus hilgardii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
6 * 40000, SDS-PAGE Lentilactobacillus hilgardii
230600
-
gel filtration Lentilactobacillus hilgardii

Organism

Organism UniProt Comment Textmining
Lentilactobacillus hilgardii Q8G998
-
-

Subunits

Subunits Comment Organism
hexamer 6 * 40000, SDS-PAGE Lentilactobacillus hilgardii