4IVI
Crystal structure of a family VIII carboxylesterase.
Summary for 4IVI
| Entry DOI | 10.2210/pdb4ivi/pdb |
| Related | 4IVK |
| Descriptor | Carboxylesterase, SULFATE ION (3 entities in total) |
| Functional Keywords | carboxylesterases beta-lactamases, helical domain and a alpha/beta domain, deep sea sediment, hydrolase |
| Biological source | uncultured bacterium |
| Total number of polymer chains | 1 |
| Total formula weight | 48444.43 |
| Authors | An, Y.J.,Kim, M.-K.,Jeong, C.-S.,Cha, S.-S. (deposition date: 2013-01-23, release date: 2013-06-19, Last modification date: 2018-01-24) |
| Primary citation | Cha, S.S.,An, Y.J.,Jeong, C.S.,Kim, M.K.,Jeon, J.H.,Lee, C.M.,Lee, H.S.,Kang, S.G.,Lee, J.H. Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase. Proteins, 81:2045-2051, 2013 Cited by PubMed Abstract: EstU1 is a unique family VIII carboxylesterase that displays hydrolytic activity toward the amide bond of clinically used β-lactam antibiotics as well as the ester bond of p-nitrophenyl esters. EstU1 assumes a β-lactamase-like modular architecture and contains the residues Ser100, Lys103, and Tyr218, which correspond to the three catalytic residues (Ser64, Lys67, and Tyr150, respectively) of class C β-lactamases. The structure of the EstU1/cephalothin complex demonstrates that the active site of EstU1 is not ideally tailored to perform an efficient deacylation reaction during the hydrolysis of β-lactam antibiotics. This result explains the weak β-lactamase activity of EstU1 compared with class C β-lactamases. Finally, structural and sequential comparison of EstU1 with other family VIII carboxylesterases elucidates an operative molecular strategy used by family VIII carboxylesterases to extend their substrate spectrum. PubMed: 23737193DOI: 10.1002/prot.24334 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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