2AJZ
Crystal Structure of Cocaine catalytic Antibody 7A1 Fab' in Complex with ecgonine methyl ester
Summary for 2AJZ
| Entry DOI | 10.2210/pdb2ajz/pdb |
| Related | 2AJS 2AJU 2AJV 2AJX 2AJY 2AK1 |
| Descriptor | Antibody 7A1 Fab', 3-HYDROXY-8-METHYL-8-AZA-BICYCLO[3.2.1]OCTANE-2-CARBOXYLIC ACID METHYL ESTER, ... (4 entities in total) |
| Functional Keywords | catalytic antibody, fab, ecgonine methyl ester, hydrolytic, immune system |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 4 |
| Total formula weight | 96249.28 |
| Authors | Zhu, X.,Wilson, I.A. (deposition date: 2005-08-02, release date: 2006-02-14, Last modification date: 2024-10-30) |
| Primary citation | Zhu, X.,Dickerson, T.J.,Rogers, C.J.,Kaufmann, G.F.,Mee, J.M.,McKenzie, K.M.,Janda, K.D.,Wilson, I.A. Complete reaction cycle of a cocaine catalytic antibody at atomic resolution. Structure, 14:205-216, 2006 Cited by PubMed Abstract: Antibody 7A1 hydrolyzes cocaine to produce nonpsychoactive metabolites ecgonine methyl ester and benzoic acid. Crystal structures of 7A1 Fab' and six complexes with substrate cocaine, the transition state analog, products ecgonine methyl ester and benzoic acid together and individually, as well as heptaethylene glycol have been analyzed at 1.5-2.3 angstroms resolution. Here, we present snapshots of the complete cycle of the cocaine hydrolytic reaction at atomic resolution. Significant structural rearrangements occur along the reaction pathway, but they are generally limited to the binding site, including the ligands themselves. Several interacting side chains either change their rotamers or alter their mobility to accommodate the different reaction steps. CDR loop movements (up to 2.3 angstroms) and substantial side chain rearrangements (up to 9 angstroms) alter the shape and size (approximately 320-500 angstroms3) of the antibody active site from "open" to "closed" to "open" for the substrate, transition state, and product states, respectively. PubMed: 16472740DOI: 10.1016/j.str.2005.10.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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