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.

1y62

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 16:23, 3 November 2021

A 2.4 crystal structure of conkunitzin-S1, a novel Kunitz-fold cone snail neurotoxin.

Structural highlights

1y62 is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Cone snails (Conus) are predatory marine mollusks that immobilize prey with venom containing 50-200 neurotoxic polypeptides. Most of these polypeptides are small disulfide-rich conotoxins that can be classified into families according to their respective ion-channel targets and patterns of cysteine-cysteine disulfides. Conkunitzin-S1, a potassium-channel pore-blocking toxin isolated from C. striatus venom, is a member of a newly defined conotoxin family with sequence homology to Kunitz-fold proteins such as alpha-dendrotoxin and bovine pancreatic trypsin inhibitor (BPTI). While conkunitzin-S1 and alpha-dendrotoxin are 42% identical in amino-acid sequence, conkunitzin-S1 has only four of the six cysteines normally found in Kunitz proteins. Here, the crystal structure of conkunitzin-S1 is reported. Conkunitzin-S1 adopts the canonical 3(10)-beta-beta-alpha Kunitz fold complete with additional distinguishing structural features including two completely buried water molecules. The crystal structure, although completely consistent with previously reported NMR distance restraints, provides a greater degree of precision for atomic coordinates, especially for S atoms and buried solvent molecules. The region normally cross-linked by cysteines II and IV in other Kunitz proteins retains a network of hydrogen bonds and van der Waals interactions comparable to those found in alpha-dendrotoxin and BPTI. In conkunitzin-S1, glycine occupies the sequence position normally reserved for cysteine II and the special steric properties of glycine allow additional van der Waals contacts with the glutamine residue substituting for cysteine IV. Evolution has thus defrayed the cost of losing a disulfide bond by augmenting and optimizing weaker yet nonetheless effective non-covalent interactions.

Structure of conkunitzin-S1, a neurotoxin and Kunitz-fold disulfide variant from cone snail.,Dy CY, Buczek P, Imperial JS, Bulaj G, Horvath MP Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):980-90. Epub 2006, Aug 19. PMID:16929098^[1]

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

References

↑ Dy CY, Buczek P, Imperial JS, Bulaj G, Horvath MP. Structure of conkunitzin-S1, a neurotoxin and Kunitz-fold disulfide variant from cone snail. Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):980-90. Epub 2006, Aug 19. PMID:16929098 doi:http://dx.doi.org/10.1107/S0907444906021123

1 Structural highlights
2 Evolutionary Conservation
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/1y62"

@@ Line 3: / Line 3: @@
 <StructureSection load='1y62' size='340' side='right'caption='[[1y62]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1y62]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y62 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y62 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1y62]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y62 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y62 OCA], [http://pdbe.org/1y62 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y62 RCSB], [http://www.ebi.ac.uk/pdbsum/1y62 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y62 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=1y62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y62 OCA], [https://pdbe.org/1y62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y62 RCSB], [https://www.ebi.ac.uk/pdbsum/1y62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y62 ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

1y62

From Proteopedia

Revision as of 16:23, 3 November 2021

A 2.4 crystal structure of conkunitzin-S1, a novel Kunitz-fold cone snail neurotoxin.

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox