1ym0

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spinqualitylabelsall models 1ym0, resolution 2.06Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Earthworm Fibrinolytic Enzyme Component B: a Novel, Glycosylated Two-chained Trypsin

Overview

The earthworm fibrinolytic enzyme (EFE), belonging to a group of serine, proteases with strong fibrinolytic activity, has been used in a mixture as, an oral drug for prevention and treatment of thrombosis in East Asia. The, EFE component b (EFE-b) is one of seven EFE components from Eisenia, fetida, and among them it has nearly the highest fibrinolytic activity., Here, we report its crystal structure at a resolution of 2.06A. The, structural analysis shows that EFE-b should be classified as a trypsin, from earthworm. However, it is distinct from other trypsins. It is a, two-chained protease with an N-terminal, pyroglutamated light chain and an, N-glycosylated heavy chain. Furthermore, the heavy chain contains a novel, structural motif, an eight-membered ring resulting from a disulfide bridge, between two neighboring cysteine residues, and a cis peptide bond exists, between these two cysteine residues. The crystal structure of EFE-b, provides the structural basis for its high level of stability and reveals, its complicated post-translational modifications in earthworm. This, structure is the first reported for a glycosylated two-chained trypsin, which may provide useful clues to explain the origin and evolution of the, chymotrypsin family.

About this Structure

1YM0 is a Protein complex structure of sequences from Eisenia fetida with MG and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of earthworm fibrinolytic enzyme component B: a novel, glycosylated two-chained trypsin., Wang F, Wang C, Li M, Zhang JP, Gui LL, An XM, Chang WR, J Mol Biol. 2005 May 6;348(3):671-85. PMID:15826663

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