1ym0: Difference between revisions

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Template:STRUCTURE 1ym0

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

Template:ABSTRACT PUBMED 15826663

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

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

Crystallization and preliminary crystallographic analysis of earthworm fibrinolytic enzyme component B from Eisenia fetida., Wang F, Wang C, Li M, Gui L, Zhang J, Chang W, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):933-5. Epub 2004, Apr 21. PMID:15103143

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 {{STRUCTURE_1ym0|  PDB=1ym0  |  SCENE=  }}
-'''Crystal Structure of Earthworm Fibrinolytic Enzyme Component B: a Novel, Glycosylated Two-chained Trypsin'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15826663}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15826663 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15826663}}
 ==About this Structure==
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 ==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:[http://www.ncbi.nlm.nih.gov/pubmed/15826663 15826663]
+Crystallization and preliminary crystallographic analysis of earthworm fibrinolytic enzyme component B from Eisenia fetida., Wang F, Wang C, Li M, Gui L, Zhang J, Chang W, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):933-5. Epub 2004, Apr 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15103143 15103143]
 [[Category: An, X M.]]
 [[Category: Chang, W R.]]
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 [[Category: Pyroglutamation]]
 [[Category: Two chain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:29:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:32:03 2008''