4RDY
Crystal structure of VmoLac bound to 3-oxo-C10 AHL
Summary for 4RDY
| Entry DOI | 10.2210/pdb4rdy/pdb |
| Related | 4RDZ 4RE0 |
| Descriptor | Parathion hydrolase, COBALT (II) ION, 3-oxo-N-[(3S)-2-oxotetrahydrofuran-3-yl]decanamide, ... (6 entities in total) |
| Functional Keywords | lactonase, quorum sensing, aryldialkylphosphatase, hydrolase |
| Biological source | Vulcanisaeta moutnovskia |
| Total number of polymer chains | 2 |
| Total formula weight | 73371.58 |
| Authors | Hiblot, J.,Bzdrenga, J.,Champion, C.,Gotthard, G.,Gonzalez, D.,Chabriere, E.,Elias, M. (deposition date: 2014-09-20, release date: 2015-02-25) |
| Primary citation | Hiblot, J.,Bzdrenga, J.,Champion, C.,Chabriere, E.,Elias, M. Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia. Sci Rep, 5:8372-8372, 2015 Cited by PubMed Abstract: A new representative of the Phosphotriesterase-Like Lactonases (PLLs) family from the hyperthermophilic crenarchaeon Vulcanisaeta moutnovskia has been characterized and crystallized. VmoLac is a native, proficient lactonase with promiscuous, low phosphotriesterase activity. VmoLac therefore represents an interesting candidate for engineering studies, with the aim of developing an efficient bacterial quorum-quenching agent. Here, we provide an extensive biochemical and kinetic characterization of VmoLac and describe the X-ray structures of the enzyme bound to a fatty acid and to its cognate substrate 3-oxo-C10 AHL (Acyl-Homoserine Lactone). The structures highlight possible structural determinants that may be involved in its extreme thermal stability (Tm = 128 °C). Moreover, the structure reveals that the substrate binding mode of VmoLac significantly differs from those of its close homologues, possibly explaining the substrate specificity of the enzyme. Finally, we describe the specific interactions between the enzyme and its substrate, and discuss the possible lactone hydrolysis mechanism of VmoLac. PubMed: 25670483DOI: 10.1038/srep08372 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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