4G2D

Crystal structure of the hyperthermophilic Sulfolobus islandicus PLL SisLac

Summary for 4G2D

Entry DOI	10.2210/pdb4g2d/pdb
Related	2vc5 2vc7 3uf9
Descriptor	Aryldialkylphosphatase, COBALT (II) ION, FE (II) ION, ... (4 entities in total)
Functional Keywords	promiscuous activities, hyperthermophilic, hydrolase, phosphotriesterase-like lactonases, quorum sensing, quorum-quenching, bioscavengers, (alpha/beta )8-barrel fold, lactonase, phosphotriesterase, lysine nz-carboxylic acid
Biological source	Sulfolobus islandicus
Total number of polymer chains	1
Total formula weight	35870.86
Authors	Gotthard, G.,Hiblot, J.,Elias, M.,Chabriere, E. (deposition date: 2012-07-11, release date: 2012-10-24, Last modification date: 2023-12-06)
Primary citation	Hiblot, J.,Gotthard, G.,Chabriere, E.,Elias, M. Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus Plos One, 7:e47028-e47028, 2012 Cited by PubMed Abstract: A new member of the Phosphotriesterase-Like Lactonases (PLL) family from the hyperthermophilic archeon Sulfolobus islandicus (SisLac) has been characterized. SisLac is a native lactonase that exhibits a high promiscuous phosphotriesterase activity. SisLac thus represents a promising target for engineering studies, exhibiting both detoxification and bacterial quorum quenching abilities, including human pathogens such as Pseudomonas aeruginosa. PubMed: 23071703 DOI: 10.1371/journal.pone.0047028 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation