1JKM

BREFELDIN A ESTERASE, A BACTERIAL HOMOLOGUE OF HUMAN HORMONE SENSITIVE LIPASE

1JKM の概要

• エントリーDOI: 10.2210/pdb1jkm/pdb
• 分子名称: BREFELDIN A ESTERASE (2 entities in total)
• 機能のキーワード: serine hydrolase, degradation of brefeldin a, alpha/beta hydrolase family
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77126.04

構造登録者

Wei, Y.,Contreras, A.J.,Sheffield, P.,Osterlund, T.,Derewenda, U.,Matern, U.O.,Derewenda, Z.S. (登録日: 1998-02-04, 公開日: 1999-02-16, 最終更新日: 2024-02-07)

主引用文献

Wei, Y.,Contreras, J.A.,Sheffield, P.,Osterlund, T.,Derewenda, U.,Kneusel, R.E.,Matern, U.,Holm, C.,Derewenda, Z.S.
Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase.
Nat.Struct.Biol., 6:340-345, 1999

PubMed Abstract: 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.

PubMed: 10201402
DOI: 10.1038/7576

実験手法

X-RAY DIFFRACTION (1.85 Å)