ArticleProtein science : a publication of the Protein Society2004
A model of the acid sphingomyelinase phosphoesterase domain based on its remote structural homolog purple acid phosphatase.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Porcine reproductive and respiratory syndrome virus upregulates SMPDL3B to promote viral replication by modulating lipid metabolism.iScience · 2023Article
- Plasma membrane damage repair is mediated by an acid sphingomyelinase in Entamoeba histolytica.PLoS pathogens · 2019Article
- Human acid sphingomyelinase structures provide insight to molecular basis of Niemann-Pick disease.Nature communications · 2016Article
- Epidemiological, clinical and biochemical characterization of the p.(Ala359Asp) SMPD1 variant causing Niemann-Pick disease type B.European journal of human genetics : EJHG · 2016Article
- The Lipid-Modifying Enzyme SMPDL3B Negatively Regulates Innate Immunity.Cell reports · 2015Article
- Sphingomyelin phosphodiesterase acid-like 3A (SMPDL3A) is a novel nucleotide phosphodiesterase regulated by cholesterol in human macrophages.The Journal of biological chemistry · 2014Article
- Regulated secretion of acid sphingomyelinase: implications for selectivity of ceramide formation.The Journal of biological chemistry · 2010Article
- Niemann-Pick disease, type B with TRAP-positive storage cells and secondary sea blue histiocytosis.European journal of histochemistry : EJH · 2009Article
- Characterization of common SMPD1 mutations causing types A and B Niemann-Pick disease and generation of mutation-specific mouse models.Molecular genetics and metabolism · 2008Article
- Structure and biological activities of beta toxin from Staphylococcus aureus.Journal of bacteriology · 2007Article
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Authors and funding
10 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Sequence profile and fold recognition methods identified mammalian purple acid phosphatase (PAP), a member of a dimetal-containing phosphoesterase (DMP) family, as a remote homolog of human acid sphingomyelinase (ASM). A model of the phosphoesterase domain of ASM was built based on its predicted secondary structure and the metal-coordinating residues of PAP. Due to the low sequence identity between ASM and PAP (approximately 15%), the highest degree of confidence in the model resides in the metal-binding motifs. The ASM model predicts residues Asp 206, Asp 278, Asn 318, His 425, and His 457 to be dimetal coordinating. A putative orientation for the phosphorylcholine head group of the ASM substrate, sphingomyelin (SM), was made based on the predicted catalysis of the phosphorus-oxygen bond in the active site of ASM and on a structural comparison of the PAP-phosphate complex to the C-reactive protein-phosphorylcholine complex. These complexes revealed similar spatial interactions between the metal-coordinating residues, the metals, and the phosphate groups, suggesting a putative orientation for the head group in ASM consistent with the mechanism considerations. A conserved sequence motif in ASM, NX3CX3N, was identified (Asn 381 to Asn 389) and is predicted to interact with the choline amine moiety in SM. The resulting ASM model suggests that the enzyme uses an SN2-type catalytic mechanism to hydrolyze SM, similar to other DMPs. His 319 in ASM is predicted to protonate the ceramide-leaving group in the catalysis of SM. The putative functional roles of several ASM Niemann-Pick missense mutations, located in the predicted phosphoesterase domain, are discussed in context to the model.
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