1wcb
From Proteopedia
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| - | [[Image:1wcb.gif|left|200px]]<br /> | + | [[Image:1wcb.gif|left|200px]]<br /><applet load="1wcb" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1wcb" size=" | + | |
caption="1wcb, resolution 2.5Å" /> | caption="1wcb, resolution 2.5Å" /> | ||
'''PLP-DEPENDENT CATALYTIC ANTIBODY 15A9 IN COMPLEX WITH ITS HAPTEN'''<br /> | '''PLP-DEPENDENT CATALYTIC ANTIBODY 15A9 IN COMPLEX WITH ITS HAPTEN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WCB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with IOD and PE1 as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 1WCB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=IOD:'>IOD</scene> and <scene name='pdbligand=PE1:'>PE1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=1:Pe1+Binding+Site+For+Chain+A'>1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transamination]] | [[Category: transamination]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:21:43 2008'' |
Revision as of 08:21, 3 February 2008
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PLP-DEPENDENT CATALYTIC ANTIBODY 15A9 IN COMPLEX WITH ITS HAPTEN
Overview
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 N-acetyl-L-lysine moiety of the hapten appears to have, selected for aromatic residues in hypervariable loop H3 (Trp-H100e and, Tyr-H100b), which, together with Lys-H96, create an anion-binding, environment in the active site. The structural situation and mutagenesis, experiments indicate that two catalytic residues facilitate the, transamination reaction of the PLP-D-alanine aldimine. The space vacated, by the absent L-lysine side chain of the hapten can be filled, in both, PLP-alanine aldimine complexes, by mobile Tyr-H100b. This group can, stabilize a hydroxide ion, which, however, abstracts the C alpha proton, only from D-alanine. Together with the absence of any residue capable of, deprotonating C alpha of L-alanine, Tyr-H100b thus underlies the, enantiomeric selectivity of 15A9. The reprotonation of C4' of PLP, the, rate-limiting step of 15A9-catalyzed transamination, is most likely, performed by a water molecule that, assisted by Lys-H96, produces a, hydroxide ion stabilized by the anion-binding environment.
About this Structure
1WCB is a Single protein structure of sequence from Mus musculus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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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