This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ym0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:11, 25 October 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ym0.gif|left|200px]]
 
-
<!--
+
==Crystal Structure of Earthworm Fibrinolytic Enzyme Component B: a Novel, Glycosylated Two-chained Trypsin==
-
The line below this paragraph, containing "STRUCTURE_1ym0", creates the "Structure Box" on the page.
+
<StructureSection load='1ym0' size='340' side='right'caption='[[1ym0]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1ym0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Eisenia_fetida Eisenia fetida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YM0 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
{{STRUCTURE_1ym0| PDB=1ym0 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ym0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ym0 OCA], [https://pdbe.org/1ym0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ym0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ym0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ym0 ProSAT]</span></td></tr>
-
 
+
</table>
-
'''Crystal Structure of Earthworm Fibrinolytic Enzyme Component B: a Novel, Glycosylated Two-chained Trypsin'''
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/Q3HR18_EISFE Q3HR18_EISFE]
-
 
+
== Evolutionary Conservation ==
-
==Overview==
+
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ym/1ym0_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ym0 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
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 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==
+
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<ref>PMID:15826663</ref>
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YM0 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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]
+
</div>
-
[[Category: An, X M.]]
+
<div class="pdbe-citations 1ym0" style="background-color:#fffaf0;"></div>
-
[[Category: Chang, W R.]]
+
== References ==
-
[[Category: Gui, L L.]]
+
<references/>
-
[[Category: Li, M.]]
+
__TOC__
-
[[Category: Wang, C.]]
+
</StructureSection>
-
[[Category: Wang, F.]]
+
[[Category: Eisenia fetida]]
-
[[Category: Zhang, J P.]]
+
[[Category: Large Structures]]
-
[[Category: Cis peptide bond]]
+
[[Category: An XM]]
-
[[Category: Eight-membered ring]]
+
[[Category: Chang WR]]
-
[[Category: Glycosylation]]
+
[[Category: Gui LL]]
-
[[Category: Pyroglutamation]]
+
[[Category: Li M]]
-
[[Category: Two chain]]
+
[[Category: Wang C]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:29:39 2008''
+
[[Category: Wang F]]
 +
[[Category: Zhang JP]]

Current revision

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

PDB ID 1ym0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools