3CN7
Crystal Structure Analysis of the Carboxylesterase PA3859 from Pseudomonas aeruginosa PAO1- MONOCLINIC CRYSTAL FORM
Summary for 3CN7
| Entry DOI | 10.2210/pdb3cn7/pdb |
| Related | 1AUO 1AUR 1FJ2 3CN9 |
| Descriptor | Carboxylesterase, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total) |
| Functional Keywords | alpha/beta hydrolase fold super-family, hydrolase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 4 |
| Total formula weight | 99270.14 |
| Authors | Pesaresi, A.,Lamba, D. (deposition date: 2008-03-25, release date: 2009-03-10, Last modification date: 2024-11-13) |
| Primary citation | Pesaresi, A.,Lamba, D. Insights into the fatty acid chain length specificity of the carboxylesterase PA3859 from Pseudomonas aeruginosa: A combined structural, biochemical and computational study. Biochimie, 92:1787-1792, 2010 Cited by PubMed Abstract: The open reading frame PA3859 of Pseudomonas aeruginosa encodes an intracellular carboxylesterase belonging to a group of microbial enzymes (EC 3.1.1.1) that catalyze the hydrolysis of aliphatic and aromatic esters with a broad substrate specificity. With few exceptions, for this class of enzymes, belonging to the α/β-hydrolase fold superfamily, very little information is available regarding their biochemical activity and in vivo function. The X-ray crystal structure of recombinant PA3859 has been determined for two crystal forms (space groups P2(1) and P2(1)2(1)2). The kinetic properties of the enzyme were studied using p-nitrophenyl esters as substrates and data fitted to a surface dilution mixed micelle kinetic model. Enzymatic assays and computational docking simulations, pinpointed the enzyme's preference for esters of palmitic and/or stearic acids and provided insights into the enzyme-substrate favorable binding modes. PubMed: 20850500DOI: 10.1016/j.biochi.2010.09.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.99 Å) |
Structure validation
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