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  • Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase
    Wei, Yunyi ...
    Brefeldin A esterase (BFAE), a detoxifying enzyme isolated from Bacillus subtilis, hydrolyzes and inactivates BFA, a potent fungal inhibitor of intracellular vesicle-dependent secretory transport and ... poliovirus RNA replication. We have solved the crystal structure of BFAE and we discovered that the previously reported amino acid sequence was in serious error due to frame shifts in the cDNA sequence. The correct sequence, inferred from the experimentally phased electron density map, revealed that BFAE is a homolog ofthe mammalian hormone sensitive lipase (HSL). It is a canonical alpha/beta hydrolase with two insertions forming the substrate binding pocket. The enzymecontains a lipase-like catalytic triad, Ser 202, Asp 308 and His 338, consistent with mutational studies that implicate the homologous Ser 424, Asp 693 and His 723 in the catalytic triad in human HSL.
    Vir: Nature structural biology. - ISSN 1072-8368 (Letn. 6, št. 4, 1999, str. 340-345)
    Vrsta gradiva - članek, sestavni del
    Leto - 1999
    Jezik - angleški
    COBISS.SI-ID - 21680089

vir: Nature structural biology. - ISSN 1072-8368 (Letn. 6, št. 4, 1999, str. 340-345)
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