1.C.4.4.3
Hemolytic lectin LSLc exhibits hemolytic and hemagglutinating activities. The structure at 2.6 Å resolution has been determined (Mancheño et al., 2005). The protein is hexameric. The monomer (35kDa) consists of two distinct modules: an N-terminal lectin module (a β-trefoil scaffold) and a pore-forming module (composed of domains 2 and 4) which resemble the β-pore-forming domains of aerolysin and ε-toxin (Mancheño et al., 2005).
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| Accession Number: | Q7Z8U9 |
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| Protein Name: | Hemolytic lectin LSLc |
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| Length: | 315 |
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| Molecular Weight: | 35233.00 |
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| Species: | Laetiporus sulphureus [5630] |
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| Location1 / Topology2 / Orientation3: |
Secreted1 |
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| Substrate |
small molecules |
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[1] “Molecular cloning, expression, and characterization of novel hemolytic lectins from the mushroom Laetiporus sulphureus, which show homology to bacterial toxins.” Tateno H. et.al. 12900403
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1: MIDIYIPPND LYFRLLGFVS QKVIYAYPFP RPDVGLSEVN DESTQQYFSL IHGTGERAGL
61: YAIKSKATGN VLFSRTHRDP YVGQDPENAR YNDNWFKIEP GKDDLSKYFR LVVPSTGTAL
121: VSRTNLEPYF WNSAQTPIRS DQYFIFLFKD MRIDKIEYDL KDGRILSSTP NVLATQTLAN
181: TSSQTQEMSF NLSQTLTQTS TFAYTAGFTI AVGTAFKAGV PIFAETEFKV DISVDNQWNW
241: GEENTFSKTC TATFSVRAGP GETVKAVSTV DSGIINVPFT AYLSSKSTGF EVTTEGIWRG
301: VSSWDLRHTL TSVTA