4gso

From Proteopedia

(Difference between revisions)

Current revision

structure of Jararacussin-I

Structural highlights

4gso is a 1 chain structure with sequence from Bothrops jararacussu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VSP1_BOTJR Thrombin-like enzyme that shows clotting activity upon human plasma. Shows specific fibrinogenolytic activity for Aalpha chain (FGA). Hydrolyzes fibrin, BAPNA and TAME, as well as chromogenic artificial substrates of the blood coagulation cascasde: S-27654 for factor X (F10), S-2302 for kallikrein (KLK), factor XIa (F11), and XIIa (F12), and S-2266 for kallikrein and factor XIa (F11). Subcutaneous injection into mice induces a mild edema. Intravenous and intramuscular injection reduce plasma fibrinogen concentration and increase the levels of fibrin(ogen) degradation products. Intramuscular injection also promotes an increase in the expression of proMMP-9, but is unable to activate it.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Snake venom serine proteinases (SVSPs) are hemostatically-active toxins that perturb the maintenance and regulation of both the blood coagulation cascade and fibrinolytic feedback system at specific points, and hence, are widely used as tools in pharmacological and clinical diagnosis. The crystal structure of a thrombin-like enzyme (TLE) from Bothrops jararacussu venom (Jararacussin-I) was determined at 2.48 A resolution. This is the first crystal structure of a TLE and permits structural comparisons with both the Agkistrodon contortrix contortrix Protein C Activator (ACC-C) and the Trimeresurus stejnegeri plasminogen activator (TSV-PA). Despite the highly conserved overall fold, significant differences in the amino acid compositions and three-dimensional conformations of the loops surrounding the active site significantly alter the molecular topography and charge distribution profile of the catalytic interface. In contrast to other SVSPs, the catalytic interface of Jararacussin-I is highly negatively charged, which contributes to its unique macromolecular selectivity.

Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes.,Ullah A, Souza TC, Zanphorlin LM, Mariutti RB, Santana VS, Murakami MT, Arni RK Protein Sci. 2012 Nov 8. doi: 10.1002/pro.2189. PMID:23139169^[4]

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

References

↑ Perez AV, Saravia P, Rucavado A, Sant'Ana CD, Soares AM, Gutierrez JM. Local and systemic pathophysiological alterations induced by a serine proteinase from the venom of the snake Bothrops jararacussu. Toxicon. 2007 Jun 1;49(7):1063-9. Epub 2007 Jan 5. PMID:17292935 doi:http://dx.doi.org/10.1016/j.toxicon.2006.12.011
↑ Sant' Ana CD, Ticli FK, Oliveira LL, Giglio JR, Rechia CG, Fuly AL, Selistre de Araujo HS, Franco JJ, Stabeli RG, Soares AM, Sampaio SV. BjussuSP-I: a new thrombin-like enzyme isolated from Bothrops jararacussu snake venom. Comp Biochem Physiol A Mol Integr Physiol. 2008 Nov;151(3):443-54. Epub 2007 Mar , 7. PMID:17466550 doi:http://dx.doi.org/10.1016/j.cbpa.2007.02.036
↑ Sant'Ana CD, Bernardes CP, Izidoro LF, Mazzi MV, Soares SG, Fuly AL, Zingali RB, Magro AJ, Braz AS, Fontes MR, Stabeli RG, Sampaio SV, Soares AM. Molecular characterization of BjussuSP-I, a new thrombin-like enzyme with procoagulant and kallikrein-like activity isolated from Bothrops jararacussu snake venom. Biochimie. 2008 Mar;90(3):500-7. Epub 2007 Oct 18. PMID:17996740 doi:http://dx.doi.org/10.1016/j.biochi.2007.10.005
↑ Ullah A, Souza TC, Zanphorlin LM, Mariutti RB, Santana VS, Murakami MT, Arni RK. Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes. Protein Sci. 2012 Nov 8. doi: 10.1002/pro.2189. PMID:23139169 doi:http://dx.doi.org/10.1002/pro.2189

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4gso"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4gso]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bothrops_jararacussu Bothrops jararacussu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GSO FirstGlance]. <br>
-</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=4gso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gso OCA], [https://pdbe.org/4gso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gso RCSB], [https://www.ebi.ac.uk/pdbsum/4gso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gso ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=4gso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gso OCA], [https://pdbe.org/4gso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gso RCSB], [https://www.ebi.ac.uk/pdbsum/4gso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gso ProSAT]</span></td></tr>
 </table>
 == Function ==

4gso

From Proteopedia

Current revision

structure of Jararacussin-I

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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