1oqs: Difference between revisions

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<StructureSection load='1oqs' size='340' side='right'caption='[[1oqs]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1oqs' size='340' side='right'caption='[[1oqs]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1oqs]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OQS FirstGlance]. <br>
<table><tr><td colspan='2'>[[1oqs]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_siamensis Daboia siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OQS FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </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]] 1.9&#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=1oqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqs OCA], [https://pdbe.org/1oqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oqs RCSB], [https://www.ebi.ac.uk/pdbsum/1oqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oqs ProSAT]</span></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=1oqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqs OCA], [https://pdbe.org/1oqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oqs RCSB], [https://www.ebi.ac.uk/pdbsum/1oqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oqs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PA2A7_DABSI PA2A7_DABSI]] Heterodimer: RV-4/RV-7 targets the presynaptic sites of the neuromuscular junction.<ref>PMID:8835338</ref>  Monomer: snake venom phospholipase A2 (PLA2) RV-7 that has low enzymatic activity and is not toxic. It inhibits the enzymatic activity of RV-4 in vitro but potentiates its lethal potency and neurotoxicity. It may facilitate the specific binding of RV-4 to its presynaptic binding sites, probably by acting as a chaperon, minimizing distraction and destruction of RV-4 en route to the site of action by reducing non-specific binding to muscle and other organs. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:8835338</ref> [[https://www.uniprot.org/uniprot/PA2B4_DABSI PA2B4_DABSI]] Heterodimer RV-4/RV-7: acts as a presynaptic neurotoxin.  Monomer: snake venom phospholipase A2 (PLA2) that acts as a presynaptic neurotoxin. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
[https://www.uniprot.org/uniprot/PA2A7_DABSI PA2A7_DABSI] Heterodimer: RV-4/RV-7 targets the presynaptic sites of the neuromuscular junction.<ref>PMID:8835338</ref>  Monomer: snake venom phospholipase A2 (PLA2) RV-7 that has low enzymatic activity and is not toxic. It inhibits the enzymatic activity of RV-4 in vitro but potentiates its lethal potency and neurotoxicity. It may facilitate the specific binding of RV-4 to its presynaptic binding sites, probably by acting as a chaperon, minimizing distraction and destruction of RV-4 en route to the site of action by reducing non-specific binding to muscle and other organs. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:8835338</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1oqs ConSurf].
</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=1oqs ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The presynaptic viperotoxin F is the major lethal component of the venom of Vipera russelli formosensis (Taiwan viper). It is a heterodimer of two highly homologous (65% identity) but oppositely charged subunits: a basic and neurotoxic PLA(2) (RV-4) and an acidic non-toxic component with a very low enzymatic activity (RV-7). The crystal structure of the complex has been determined by molecular replacement and refined to 1.9 A resolution and an R factor of 22.3% with four RV-4/RV-7 complexes in the asymmetric unit, which do not exhibit any local point-group symmetry. The complex formation decreases the accessible surface area of the two subunits by approximately 1425 A(2). Both PLA(2)s are predicted to have very low, if any, anticoagulant activity. The structure of viperotoxin F is compared with that of the heterodimeric neurotoxin vipoxin from the venom of another viper, V. ammodytes meridionalis. The structural basis for the differences between the pharmacological activities of the two toxins is discussed. The neutralization of the negative charge of the major ligand for Ca(2+), Asp49, by intersubunit salt bridges is probably a common mechanism of self-stabilization of heterodimeric Viperinae snake-venom neurotoxins in the absence of bound calcium.
Structure of the heterodimeric neurotoxic complex viperotoxin F (RV-4/RV-7) from the venom of Vipera russelli formosensis at 1.9 A resolution.,Perbandt M, Tsai IH, Fuchs A, Banumathi S, Rajashankar KR, Georgieva D, Kalkura N, Singh TP, Genov N, Betzel C Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1679-87. Epub 2003, Sep 19. PMID:14501106<ref>PMID:14501106</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1oqs" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Daboia russellii siamensis]]
[[Category: Daboia siamensis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Betzel, C]]
[[Category: Betzel C]]
[[Category: Perbandt, M]]
[[Category: Perbandt M]]
[[Category: Hydrolase]]

Revision as of 08:49, 17 April 2024

Crystal Structure of RV4/RV7 ComplexCrystal Structure of RV4/RV7 Complex

Structural highlights

1oqs is a 8 chain structure with sequence from Daboia siamensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PA2A7_DABSI Heterodimer: RV-4/RV-7 targets the presynaptic sites of the neuromuscular junction.[1] Monomer: snake venom phospholipase A2 (PLA2) RV-7 that has low enzymatic activity and is not toxic. It inhibits the enzymatic activity of RV-4 in vitro but potentiates its lethal potency and neurotoxicity. It may facilitate the specific binding of RV-4 to its presynaptic binding sites, probably by acting as a chaperon, minimizing distraction and destruction of RV-4 en route to the site of action by reducing non-specific binding to muscle and other organs. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.[2]

Evolutionary Conservation

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

See Also

References

  1. ↑ Tsai IH, Lu PJ, Su JC. Two types of Russell's viper revealed by variation in phospholipases A2 from venom of the subspecies. Toxicon. 1996 Jan;34(1):99-109. PMID:8835338
  2. ↑ Tsai IH, Lu PJ, Su JC. Two types of Russell's viper revealed by variation in phospholipases A2 from venom of the subspecies. Toxicon. 1996 Jan;34(1):99-109. PMID:8835338

1oqs, resolution 1.90Å

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