2UXY
Aliphatic amidase
Summary for 2UXY
| Entry DOI | 10.2210/pdb2uxy/pdb |
| Related | 1K17 |
| Descriptor | ALIPHATIC AMIDASE, SULFATE ION (3 entities in total) |
| Functional Keywords | nitrilase superfamily, pseudomonas aeruginosa, hydrolase, acyl transfer, thiol enzymes, hydroxamic acid, aliphatic amidase |
| Biological source | PSEUDOMONAS AERUGINOSA |
| Total number of polymer chains | 1 |
| Total formula weight | 38136.18 |
| Authors | Andrade, J.,KArmali, A.,Carrondo, M.A.,Frazao, C. (deposition date: 2007-04-02, release date: 2007-04-17, Last modification date: 2025-04-09) |
| Primary citation | Andrade, J.,Karmali, A.,Carrondo, M.A.,Frazao, C. Structure of Amidase from Pseudomonas Aeruginosa Showing a Trapped Acyl Transfer Reaction Intermediate State. J.Biol.Chem., 282:19598-, 2007 Cited by PubMed Abstract: Microbial amidases belong to the thiol nitrilases family and have potential biotechnological applications in chemical and pharmaceutical industries as well as in bioremediation. The amidase from Pseudomonas aeruginosa isa6 x 38-kDa enzyme that catalyzes the hydrolysis of a small range of short aliphatic amides. The hereby reported high resolution crystallographic structure shows that each amidase monomer is formed by a globular four-layer alphabetabetaalpha sandwich domain with an additional 81-residue long C-terminal segment. This wraps arm-in-arm with a homologous C-terminal chain of another monomer, producing a strongly packed dimer. In the crystal, the biological active homo-hexameric amidase is built grouping three such dimers around a crystallographic 3-fold axis. The structure also elucidates the structural basis for the enzyme activity, with the nitrilases catalytic triad at the bottom of a 13-A deep, funnel-shaped pocket, accessible from the solvent through a narrow neck with 3-A diameter. An acyl transfer intermediate, resulting from the purification protocol, was found bound to the amidase nucleophilic agent, Cys(166). These results suggest that some pocket defining residues should undergo conformational shifts to allow substrates and products to access and leave the catalytic pocket, for turnover to occur. PubMed: 17442671DOI: 10.1074/JBC.M701039200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
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