2cfu | pdb_00002cfu
Crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, in complex with 1-decane-sulfonic-acid.
Structural highlights
FunctionLPAKS_PSEAE Alkylsulfatase that cleaves both short and medium-length alkylsulfates, including the widely used detergent sodium dodecyl sulfate (SDS) (PubMed:16684886). Acts in vitro on primary alkylsulfates such as decyl sulfate, octyl sulfate and hexyl sulfate, but not on sulfated sugars and arylsulfates (PubMed:16684886, PubMed:23061549). The hydrolysis of SDS allows the bacterium to use SDS as a sole carbon or sulfur source (PubMed:16684886). In addition, contributes to the in vivo virulence of P.aeruginosa by playing a central role in the degradation of mucin, a glycoprotein that is the primary component of the mucus overlaying the host epithelial tissues (PubMed:31907968). Plays a role in the degradation of both protein and carbohydrate moieties in mucin via the release of sulfate from mucin, D-galactose 6-sulfate (Gal-6S) and N-acetyl-D-glucosamine 6-sulfate (GlcNAc-6S) (PubMed:31907968).[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPseudomonas aeruginosa is both a ubiquitous environmental bacterium and an opportunistic human pathogen. A remarkable metabolic versatility allows it to occupy a multitude of ecological niches, including wastewater treatment plants and such hostile environments as the human respiratory tract. P. aeruginosa is able to degrade and metabolize biocidic SDS, the detergent of most commercial personal hygiene products. We identify SdsA1 of P. aeruginosa as a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as SDS as a sole carbon or sulfur source. Homologues of SdsA1 are found in many pathogenic and some nonpathogenic bacteria. The crystal structure of SdsA1 reveals three distinct domains. The N-terminal catalytic domain with a binuclear Zn2+ cluster is a distinct member of the metallo-beta-lactamase fold family, the central dimerization domain ensures resistance to high concentrations of SDS, whereas the C-terminal domain provides a hydrophobic groove, presumably to recruit long aliphatic substrates. Crystal structures of apo-SdsA1 and complexes with substrate analog and products indicate an enzymatic mechanism involving a water molecule indirectly activated by the Zn2+ cluster. The enzyme SdsA1 thus represents a previously undescribed class of sulfatases that allows P. aeruginosa to survive and thrive under otherwise bacteriocidal conditions. The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases.,Hagelueken G, Adams TM, Wiehlmann L, Widow U, Kolmar H, Tummler B, Heinz DW, Schubert WD Proc Natl Acad Sci U S A. 2006 May 16;103(20):7631-6. Epub 2006 May 9. PMID:16684886[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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