The three domains of a bacterial sialidase: a β-propeller, an immunoglobulin module and a galactose-binding jelly-roll

Gaskell, A.; Crennell, S.J.; Taylor, G.L.

doi:10.1016/s0969-2126(01)00255-6

Cited by 204 publications

(203 citation statements)

References 41 publications

(48 reference statements)

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“…Previously proposed prokaryotic examples of the IgSF have been recognized on the basis of similar folding topologies, but their sequence similarity to eukaryotic IgSF members has been so low as to raise questions of possible evolution from two independent ancestors (Hofmann et al, 1989; Bork et al, 1994;Gaskell et al, 1995). We have detected these domains based solely on sequence similarities, and thus feel confident drawing a conclusion of divergent evolution.…”

Section: Rhqvtttk-----ykstfeissvqasdegnyswvens-egkq-eaeftltiqmentioning

confidence: 60%

Members of the immunoglobulin superfamily in bacteria

1996

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Abstract:We report a prediction that two prokaryotic proteins contain immunoglobulin superfamily domains. Immunoglobulinlike folds have been identified previously in prokaryotic proteins, but these share no recognizable sequence similarity with eukaryotic immunoglobulin superfamily (IgSF) folds, and may be the result of the physics and chemistry of proteins favoring certain common folds. In contrast, the prokaryotic proteins identified have sequences whose match to the immunoglobulin superfamily can be detected by hidden Markov modeling, BLASTP matches, key residue analysis, and secondary structure predictions. We propose that these prokaryotic immunoglobulin-like domains are almost certain to be related by divergence from a common ancestor to eukaryotic immunoglobulin superfamily domains.

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Section: Rhqvtttk-----ykstfeissvqasdegnyswvens-egkq-eaeftltiqmentioning

confidence: 60%

Members of the immunoglobulin superfamily in bacteria

1996

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“…The fold comprises predominantly coil, but does have two small β-sheets and a small region of helix ( Figure 1). This fold can accommodate a surprisingly extended binding site as exemplified by WGA, [52]); (e) family 2 CBM, Cf CBM2, from Cellulomonas fimi (PDB code 1EXG [81]); (f) family 9 CBM, TmCBM9-2, from T. maritima in complex with cellobiose (PDB code 1I82 [33]); (g) family 32 CBM, MvCBM32, from Micromonospora viridifaciens in complex with galactose (PDB code 1EUU [65]); (h) family 5 CBM, EcCBM5, from Erwinia chrysanthemi (PDB code 1AIW [82]); (i) family 13 CBM, SlCBM13, from S. lividans in complex with xylopentaose (PDB code 1MC9 [48]); (j) family 1 CBM, TrCBM1, from Trichoderma reesi (PDB code 1CBH [83]); (k) family 10 CBM, CjCBM10, from Cellvibrio japonicus (PDB code 1E8R [84]); (l) family 18 CBM from Urtica dioca in complex with chitotriose (PDB code 1EN2 [85]); (m) family 14 CBM, tachychitin, from Tachypleus tridentatus (PDB code 1DQC [86]). Bound ligands are shown as 'liquorice' representations, while bound metal ions are shown as a blue spheres.…”

Section: Hevein Foldmentioning

confidence: 99%

“…In general, this family of CBMs is found exclusively in xylanases, and this particular CBM from T. maritima has the remarkable property of recognizing the reducing end sugars of xylans and cellulose. Family 32 is a relatively new CBM family whose only currently (partially) characterized member is the C-terminal module from the Micromonospora viridifaciens sialidase [61,65]. This CBM has a very similar fold to the fucose-specific lectin from Anguilla anguilla and appears to bind galactose [61].…”

Section: Type C Small-sugar-binding Cbmsmentioning

confidence: 99%

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Boraston

Bolam

Gilbert

et al. 2004

Biochemical Journal

1,796

1,724

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The enzymic degradation of insoluble polysaccharides is one of the most important reactions on earth. Despite this, glycoside hydrolases attack such polysaccharides relatively inefficiently as their target glycosidic bonds are often inaccessible to the active site of the appropriate enzymes. In order to overcome these problems, many of the glycoside hydrolases that utilize insoluble substrates are modular, comprising catalytic modules appended to one or more non-catalytic CBMs (carbohydrate-binding modules). CBMs promote the association of the enzyme with the substrate. In view of the central role that CBMs play in the enzymic hydrolysis of plant structural and storage polysaccharides, the ligand specificity displayed by these protein modules and the mechanism by which they recognize their target carbohydrates have received considerable attention since their discovery almost 20 years ago. In the last few years, CBM research has harnessed structural, functional and bioinformatic approaches to elucidate the molecular determinants that drive CBM-carbohydrate recognition. The present review summarizes the impact structural biology has had on our understanding of the mechanisms by which CBMs bind to their target ligands.

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“…Active site residues are shown as black on yellow; ''Asp-box'' repeats are shown as black on blue; and novel missense mutations identi¢ed in the human sialidase gene are shown as black on pink. The b-sheets in the structures of bacterial sialidases [Gaskell et al,1995;Crennell et al,1993Crennell et al, ,1994 are indicated by arrows above the alignment.…”

Section: Missense Mutationsmentioning

confidence: 99%

Molecular pathology of NEU1 gene in sialidosis

Poupětová²,

et al. 2003

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Communicated by Mark H. PaalmanLysosomal sialidase (EC 3.2.1.18) has a dual physiological function; it participates in intralysosomal catabolism of sialylated glycoconjugates and is involved in cellular immune response. Mutations in the sialidase gene NEU1, located on chromosome 6p21.3, result in autosomal recessive disorder, sialidosis, which is characterized by the progressive lysosomal storage of sialylated glycopeptides and oligosaccharides. Sialidosis type I is a milder, late-onset, normosomatic form of the disorder. Type I patients develop visual defects, myoclonus syndrome, cherry-red macular spots, ataxia, hyperreflexia, and seizures. The severe early-onset form, sialidosis type II, is also associated with dysostosis multiplex, Hurler-like phenotype, mental retardation, and hepatosplenomegaly. We summarize information on the 34 unique mutations determined so far in the sialidase gene, including four novel missense and one novel nonsense mutations found in two Czech and two French sialidosis patients. The analysis of sialidase mutations in sialidosis revealed considerable molecular heterogeneity, reflecting the diversity of clinical phenotypes that make molecular diagnosis difficult. The majority of sialidosis patients have had missense mutations, many of which have been expressed; their effects on activity, stability, intracellular localization, and supramolecular organization of sialidase were studied. A structural model of sialidase allowed us to localize mutations in the sialidase molecule and to predict their impact on the tertiary structure and biochemical properties of the enzyme. Hum Mutat 22:343-352,

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The three domains of a bacterial sialidase: a β-propeller, an immunoglobulin module and a galactose-binding jelly-roll

Cited by 204 publications

References 41 publications

Members of the immunoglobulin superfamily in bacteria

Members of the immunoglobulin superfamily in bacteria

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Molecular pathology of NEU1 gene in sialidosis

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