4ZI5
Crystal Structure of Dienelactone Hydrolase-like Promiscuous Phospotriesterase P91 from Metagenomic Libraries
Summary for 4ZI5
| Entry DOI | 10.2210/pdb4zi5/pdb |
| Descriptor | P91, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | metagenomic libraries, alpha/beta hydrolase, promiscuity, phosphotriesterase, hydrolase |
| Biological source | metagenome |
| Total number of polymer chains | 2 |
| Total formula weight | 53818.33 |
| Authors | Colin, P.-Y.,Fischer, G.,Hyvonen, M.,Hollfelder, F. (deposition date: 2015-04-27, release date: 2016-02-17, Last modification date: 2024-01-10) |
| Primary citation | Colin, P.Y.,Kintses, B.,Gielen, F.,Miton, C.M.,Fischer, G.,Mohamed, M.F.,Hyvonen, M.,Morgavi, D.P.,Janssen, D.B.,Hollfelder, F. Ultrahigh-throughput discovery of promiscuous enzymes by picodroplet functional metagenomics. Nat Commun, 6:10008-10008, 2015 Cited by PubMed Abstract: Unculturable bacterial communities provide a rich source of biocatalysts, but their experimental discovery by functional metagenomics is difficult, because the odds are stacked against the experimentor. Here we demonstrate functional screening of a million-membered metagenomic library in microfluidic picolitre droplet compartments. Using bait substrates, new hydrolases for sulfate monoesters and phosphotriesters were identified, mostly based on promiscuous activities presumed not to be under selection pressure. Spanning three protein superfamilies, these break new ground in sequence space: promiscuity now connects enzymes with only distantly related sequences. Most hits could not have been predicted by sequence analysis, because the desired activities have never been ascribed to similar sequences, showing how this approach complements bioinformatic harvesting of metagenomic sequencing data. Functional screening of a library of unprecedented size with excellent assay sensitivity has been instrumental in identifying rare genes constituting catalytically versatile hubs in sequence space as potential starting points for the acquisition of new functions. PubMed: 26639611DOI: 10.1038/ncomms10008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.702 Å) |
Structure validation
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