1jkm
From Proteopedia
BREFELDIN A ESTERASE, A BACTERIAL HOMOLOGUE OF HUMAN HORMONE SENSITIVE LIPASE
Overview
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 of the mammalian hormone sensitive lipase (HSL). It is a canonical alpha/beta hydrolase with two insertions forming the substrate binding pocket. The enzyme contains 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.
About this Structure
1JKM is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase., Wei Y, Contreras JA, Sheffield P, Osterlund T, Derewenda U, Kneusel RE, Matern U, Holm C, Derewenda ZS, Nat Struct Biol. 1999 Apr;6(4):340-5. PMID:10201402 Page seeded by OCA on Fri May 2 21:20:16 2008
