1JFR

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

Summary for 1JFR

• Entry DOI: 10.2210/pdb1jfr/pdb
• Descriptor: LIPASE (2 entities in total)
• Functional Keywords: serine hydrolase, lipase
• Biological source: Streptomyces exfoliatus
• Total number of polymer chains: 2
• Total formula weight: 55934.28

Authors

Wei, Y.,Derewenda, Z.S. (deposition date: 1997-07-11, release date: 1998-07-15, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)