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[[Image:1op2.gif|left|200px]]
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{{STRUCTURE_1op2|  PDB=1op2  |  SCENE=  }}
'''Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus'''


==Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus==
<StructureSection load='1op2' size='340' side='right'caption='[[1op2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1op2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OP2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1op2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1op2 OCA], [https://pdbe.org/1op2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1op2 RCSB], [https://www.ebi.ac.uk/pdbsum/1op2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1op2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VSPP_DEIAC VSPP_DEIAC] Snake venom serine protease that has fibrinogenolytic activities. Also possess esterolysis and amidolytic activities.<ref>PMID:12595722</ref> <ref>PMID:15632114</ref>
== Evolutionary Conservation ==
[[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/op/1op2_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=1op2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We deduced that Agkistrodon actus venom serine proteinases I and II, previously isolated from the venom of A. acutus (Zhu, Z., Gong, P., Teng, M., and Niu, L. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 547-550), are encoded by two almost identical genes, with only the single substitution Asp for Asn at residue 62. Amidolytic assays indicated that they possess slightly different enzymatic properties. Crystal structures of A. actus venom serine proteinases I and II were determined at resolution of 2.0 and 2.1 A with the identification of trisaccharide (NAG(301)-FUC(302)-NAG(303)) and monosaccharide (NAG(301)) residues in them, respectively. The substrate binding sites S3 of the two proteinases appear much shallower than that of Trimeresurus stejnegeri venom plasminogen activator despite the overall structural similarity. Based on structural analysis, we showed that these Asn(35)-linked oligosaccharides collide spatially with some inhibitors, such as soybean trypsin inhibitor, and would therefore hinder their inhibitory binding. Difference of the carbohydrates in both the proteinases might also lead to their altered catalytic activities.


==Overview==
Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases.,Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L J Biol Chem. 2005 Mar 18;280(11):10524-9. Epub 2005 Jan 4. PMID:15632114<ref>PMID:15632114</ref>
We deduced that Agkistrodon actus venom serine proteinases I and II, previously isolated from the venom of A. acutus (Zhu, Z., Gong, P., Teng, M., and Niu, L. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 547-550), are encoded by two almost identical genes, with only the single substitution Asp for Asn at residue 62. Amidolytic assays indicated that they possess slightly different enzymatic properties. Crystal structures of A. actus venom serine proteinases I and II were determined at resolution of 2.0 and 2.1 A with the identification of trisaccharide (NAG(301)-FUC(302)-NAG(303)) and monosaccharide (NAG(301)) residues in them, respectively. The substrate binding sites S3 of the two proteinases appear much shallower than that of Trimeresurus stejnegeri venom plasminogen activator despite the overall structural similarity. Based on structural analysis, we showed that these Asn(35)-linked oligosaccharides collide spatially with some inhibitors, such as soybean trypsin inhibitor, and would therefore hinder their inhibitory binding. Difference of the carbohydrates in both the proteinases might also lead to their altered catalytic activities.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1OP2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OP2 OCA].
</div>
<div class="pdbe-citations 1op2" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases., Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L, J Biol Chem. 2005 Mar 18;280(11):10524-9. Epub 2005 Jan 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15632114 15632114]
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Deinagkistrodon acutus]]
[[Category: Deinagkistrodon acutus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Niu, L.]]
[[Category: Niu L]]
[[Category: Teng, M.]]
[[Category: Teng M]]
[[Category: Zhu, Z.]]
[[Category: Zhu Z]]
[[Category: Agkistrodon acutus]]
[[Category: Glycoprotein]]
[[Category: Serine proteinase]]
[[Category: Snake venom]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:06:57 2008''

Latest revision as of 10:33, 23 October 2024

Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutusCrystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus

Structural highlights

1op2 is a 1 chain structure with sequence from Deinagkistrodon acutus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VSPP_DEIAC Snake venom serine protease that has fibrinogenolytic activities. Also possess esterolysis and amidolytic activities.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We deduced that Agkistrodon actus venom serine proteinases I and II, previously isolated from the venom of A. acutus (Zhu, Z., Gong, P., Teng, M., and Niu, L. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 547-550), are encoded by two almost identical genes, with only the single substitution Asp for Asn at residue 62. Amidolytic assays indicated that they possess slightly different enzymatic properties. Crystal structures of A. actus venom serine proteinases I and II were determined at resolution of 2.0 and 2.1 A with the identification of trisaccharide (NAG(301)-FUC(302)-NAG(303)) and monosaccharide (NAG(301)) residues in them, respectively. The substrate binding sites S3 of the two proteinases appear much shallower than that of Trimeresurus stejnegeri venom plasminogen activator despite the overall structural similarity. Based on structural analysis, we showed that these Asn(35)-linked oligosaccharides collide spatially with some inhibitors, such as soybean trypsin inhibitor, and would therefore hinder their inhibitory binding. Difference of the carbohydrates in both the proteinases might also lead to their altered catalytic activities.

Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases.,Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L J Biol Chem. 2005 Mar 18;280(11):10524-9. Epub 2005 Jan 4. PMID:15632114[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Zhu Z, Gong P, Teng M, Niu L. Purification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom. Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):547-50. Epub 2003, Feb 21. PMID:12595722
  2. ↑ Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L. Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases. J Biol Chem. 2005 Mar 18;280(11):10524-9. Epub 2005 Jan 4. PMID:15632114 doi:10.1074/jbc.M412900200
  3. ↑ Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L. Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases. J Biol Chem. 2005 Mar 18;280(11):10524-9. Epub 2005 Jan 4. PMID:15632114 doi:10.1074/jbc.M412900200

1op2, resolution 2.10Å

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