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Lookup NU author(s): Amy Openshaw, Professor Paul RaceORCiD, Dr Mark Banfield
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Sphingomyelinases C are enzymes that catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine. Various pathogenic bacteria produce secreted neutral sphingomyelinases C that act as membrane-damaging virulence factors. Mammalian neutral sphingomyelinases C, which display sequence homology to the bacterial enzymes, are involved in sphingolipid metabolism and signaling. This article describes the first structure to be determined for a member of the neutral sphingomyelinase C family, SmcL, from the intracellular bacterial pathogen Listeria ivanovii. The structure has been refined to 1.9-Å resolution with phases derived by single isomorphous replacement with anomalous scattering techniques from a single iridium derivative. SmcL adopts a DNase I-like fold, and is the first member of this protein superfamily to have its structure determined that acts as a phospholipase. The structure reveals several unique features that adapt the protein to its phospholipid substrate. These include large hydrophobic β-hairpin and hydrophobic loops surrounding the active site that may bind and penetrate the lipid bilayer to position sphingomyelin in a catalytically competent position. The structure also provides insight into the proposed general base/acid catalytic mechanism, in which His-325 and His-185 play key roles. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
Author(s): Openshaw AEA, Race PR, Monzo HJ, Vazquez-Boland J-A, Banfield MJ
Publication type: Article
Publication status: Published
Journal: Journal of Biological Chemistry
Year: 2005
Volume: 280
Issue: 41
Pages: 35011-35017
Print publication date: 14/10/2005
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology, Inc.
URL: http://dx.doi.org/10.1074/jbc.M506800200
DOI: 10.1074/jbc.M506800200
PubMed id: 16093240
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