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[[Image:1ym0.gif|left|200px]]


{{Structure
==Crystal Structure of Earthworm Fibrinolytic Enzyme Component B: a Novel, Glycosylated Two-chained Trypsin==
|PDB= 1ym0 |SIZE=350|CAPTION= <scene name='initialview01'>1ym0</scene>, resolution 2.06&Aring;
<StructureSection load='1ym0' size='340' side='right'caption='[[1ym0]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <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>
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ym0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ym0 OCA], [http://www.ebi.ac.uk/pdbsum/1ym0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ym0 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/Q3HR18_EISFE Q3HR18_EISFE]
 
== Evolutionary Conservation ==
'''Crystal Structure of Earthworm Fibrinolytic Enzyme Component B: a Novel, Glycosylated Two-chained Trypsin'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <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/initialview03.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>
1YM0 is a [[Protein complex]] structure of sequences from [http://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].


==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>
<div class="pdbe-citations 1ym0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Eisenia fetida]]
[[Category: Eisenia fetida]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: An, X M.]]
[[Category: An XM]]
[[Category: Chang, W R.]]
[[Category: Chang WR]]
[[Category: Gui, L L.]]
[[Category: Gui LL]]
[[Category: Li, M.]]
[[Category: Li M]]
[[Category: Wang, C.]]
[[Category: Wang C]]
[[Category: Wang, F.]]
[[Category: Wang F]]
[[Category: Zhang, J P.]]
[[Category: Zhang JP]]
[[Category: cis peptide bond]]
[[Category: eight-membered ring]]
[[Category: glycosylation]]
[[Category: pyroglutamation]]
[[Category: two chain]]
 
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