1ym0

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(New page: 200px<br /><applet load="1ym0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ym0, resolution 2.06&Aring;" /> '''Crystal Structure of...)
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[[Image:1ym0.gif|left|200px]]<br /><applet load="1ym0" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ym0.gif|left|200px]]<br /><applet load="1ym0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ym0, resolution 2.06&Aring;" />
caption="1ym0, resolution 2.06&Aring;" />
'''Crystal Structure of Earthworm Fibrinolytic Enzyme Component B: a Novel, Glycosylated Two-chained Trypsin'''<br />
'''Crystal Structure of Earthworm Fibrinolytic Enzyme Component B: a Novel, Glycosylated Two-chained Trypsin'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1YM0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Eisenia_fetida Eisenia fetida] with MG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YM0 OCA].
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1YM0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Eisenia_fetida Eisenia fetida] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YM0 OCA].
==Reference==
==Reference==
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[[Category: Eisenia fetida]]
[[Category: Eisenia fetida]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: An, X.M.]]
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[[Category: An, X M.]]
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[[Category: Chang, W.R.]]
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[[Category: Chang, W R.]]
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[[Category: Gui, L.L.]]
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[[Category: Gui, L L.]]
[[Category: Li, M.]]
[[Category: Li, M.]]
[[Category: Wang, C.]]
[[Category: Wang, C.]]
[[Category: Wang, F.]]
[[Category: Wang, F.]]
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[[Category: Zhang, J.P.]]
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[[Category: Zhang, J P.]]
[[Category: MG]]
[[Category: MG]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: two chains]]
[[Category: two chains]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:19:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:42 2008''

Revision as of 14:06, 21 February 2008


1ym0, resolution 2.06Å

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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 and 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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