1JFR

CRYSTAL STRUCTURE OF THE STREPTOMYCES EXFOLIATUS LIPASE AT 1.9A RESOLUTION: A MODEL FOR A FAMILY OF PLATELET-ACTIVATING FACTOR ACETYLHYDROLASES

1JFR の概要

• エントリーDOI: 10.2210/pdb1jfr/pdb
• 分子名称: LIPASE (2 entities in total)
• 機能のキーワード: serine hydrolase, lipase
• 由来する生物種: Streptomyces exfoliatus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55934.28

構造登録者

Wei, Y.,Derewenda, Z.S. (登録日: 1997-07-11, 公開日: 1998-07-15, 最終更新日: 2024-10-16)

主引用文献

Wei, Y.,Swenson, L.,Castro, C.,Derewenda, U.,Minor, W.,Arai, H.,Aoki, J.,Inoue, K.,Servin-Gonzalez, L.,Derewenda, Z.S.
Structure of a microbial homologue of mammalian platelet-activating factor acetylhydrolases: Streptomyces exfoliatus lipase at 1.9 A resolution.
Structure, 6:511-519, 1998

PubMed Abstract: Neutral lipases are ubiquitous and diverse enzymes. The molecular architecture of the structurally characterized lipases is similar, often despite a lack of detectable homology at the sequence level. Some of the microbial lipases are evolutionarily related to physiologically important mammalian enzymes. For example, limited sequence similarities were recently noted for the Streptomyces exfoliatus lipase (SeL) and two mammalian platelet-activating factor acetylhydrolases (PAF-AHs). The determination of the crystal structure of SeL allowed us to explore the structure-function relationships in this novel family of homologous hydrolases.

PubMed: 9562561
DOI: 10.1016/S0969-2126(98)00052-5

実験手法

X-RAY DIFFRACTION (1.9 Å)