4I3F

Crystal structure of serine hydrolase CCSP0084 from the polyaromatic hydrocarbon (PAH)-degrading bacterium Cycloclasticus zankles

Summary for 4I3F

• Entry DOI: 10.2210/pdb4i3f/pdb
• Descriptor: serine hydrolase CCSP0084, CHLORIDE ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: alpha and beta proteins, alpha/beta hydrolase fold, alpha/beta-hydrolases superfamily, carbon-carbon bond hydrolase family, serine hydrolase, esterase, meta-cleavage product (mcp) hydrolase, hydrolase
• Biological source: Cycloclasticus sp. P1 (Cycloclasticus zancles)
• Total number of polymer chains: 1
• Total formula weight: 34212.23

Authors

Stogios, P.J.,Xu, X.,Dong, A.,Cui, H.,Alcaide, M.,Tornes, J.,Gertler, C.,Yakimov, M.M.,Golyshin, P.N.,Ferrer, M.,Savchenko, A. (deposition date: 2012-11-26, release date: 2013-06-26, Last modification date: 2023-09-20)

Primary citation

Alcaide, M.,Tornes, J.,Stogios, P.J.,Xu, X.,Gertler, C.,Di Leo, R.,Bargiela, R.,Lafraya, A.,Guazzaroni, M.E.,Lopez-Cortes, N.,Chernikova, T.N.,Golyshina, O.V.,Nechitaylo, T.Y.,Plumeier, I.,Pieper, D.H.,Yakimov, M.M.,Savchenko, A.,Golyshin, P.N.,Ferrer, M.
Single residues dictate the co-evolution of dual esterases: MCP hydrolases from the alpha / beta hydrolase family.
Biochem.J., 454:157-166, 2013

PubMed Abstract: Several members of the C-C MCP (meta-cleavage product) hydrolase family demonstrate an unusual ability to hydrolyse esters as well as the MCPs (including those from mono- and bi-cyclic aromatics). Although the molecular mechanisms responsible for such substrate promiscuity are starting to emerge, the full understanding of these complex enzymes is far from complete. In the present paper, we describe six distinct α/β hydrolases identified through genomic approaches, four of which demonstrate the unprecedented characteristic of activity towards a broad spectrum of substrates, including p-nitrophenyl, halogenated, fatty acyl, aryl, glycerol, cinnamoyl and carbohydrate esters, lactones, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate and 2-hydroxy-6-oxohepta-2,4-dienoate. Using structural analysis and site-directed mutagenesis we have identified the three residues (Ser32, Val130 and Trp144) that determine the unusual substrate specificity of one of these proteins, CCSP0084. The results may open up new research avenues into comparative catalytic models, structural and mechanistic studies, and biotechnological applications of MCP hydrolases.

PubMed: 23750508
DOI: 10.1042/BJ20130552

Experimental method

X-RAY DIFFRACTION (1.69 Å)