2bmk
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FAB FRAGMENT OF PLP-DEPENDENT CATALYTIC ANTIBODY 15A9 IN COMPLEX WITH PHOSPHOPYRIDOXYL-D-ALANINE
OverviewOverview
Antibody 15A9, raised with 5'-phosphopyridoxyl, (PPL)-N(epsilon)-acetyl-L-lysine as hapten, catalyzes the reversible, transamination of hydrophobic D-amino acids with pyridoxal 5'-phosphate, (PLP). The crystal structures of the complexes of Fab 15A9 with, PPL-L-alanine, PPL-D-alanine, and the hapten were determined at 2.3, 2.3, and 2.5A resolution, respectively, and served for modeling the complexes, with the corresponding planar imine adducts. The conformation of the, PLP-amino acid adduct and its interactions with 15A9 are similar to those, occurring in PLP-dependent enzymes, except that the amino acid substrate, is only weakly bound, and, due to the immunization and selection strategy, the lysine residue that covalently binds PLP in these enzymes is missing., However, the ... [(full description)]
About this StructureAbout this Structure
2BMK is a [Single protein] structure of sequence from [Mus musculus] with IOD and PDD as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Structural basis for D-amino acid transamination by the pyridoxal 5'-phosphate-dependent catalytic antibody 15A9., Golinelli-Pimpaneau B, Luthi C, Christen P, J Biol Chem. 2006 Aug 18;281(33):23969-77. Epub 2006 Jun 21. PMID:16790434
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