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| | <StructureSection load='6o0d' size='340' side='right'caption='[[6o0d]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6o0d' size='340' side='right'caption='[[6o0d]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6o0d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O0D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O0D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6o0d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lithobates_catesbeianus Lithobates catesbeianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O0D FirstGlance]. <br> |
| - | </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=6o0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o0d OCA], [http://pdbe.org/6o0d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o0d RCSB], [http://www.ebi.ac.uk/pdbsum/6o0d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o0d 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]] 2.5Å</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=6o0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o0d OCA], [https://pdbe.org/6o0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o0d RCSB], [https://www.ebi.ac.uk/pdbsum/6o0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o0d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SAX_LITCT SAX_LITCT]] Binds specifically to the neurotoxin saxitoxin. Its physiological role may be to transport or sequester an endogenous organic molecule other than Fe(3+). It may participate in a detoxification mechanism for neutralizing a microbial toxin. | + | [https://www.uniprot.org/uniprot/SAX_AQUCT SAX_AQUCT] Binds specifically to the neurotoxin saxitoxin. Its physiological role may be to transport or sequester an endogenous organic molecule other than Fe(3+). It may participate in a detoxification mechanism for neutralizing a microbial toxin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lolicato, M]] | + | [[Category: Lithobates catesbeianus]] |
| - | [[Category: Minor, D L]] | + | [[Category: Lolicato M]] |
| - | [[Category: Yen, T J]] | + | [[Category: Minor DL]] |
| - | [[Category: Antitoxin]] | + | [[Category: Yen TJ]] |
| - | [[Category: Paralytic shellfish poisoning]]
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| - | [[Category: Saxitoxin]]
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| Structural highlights
Function
SAX_AQUCT Binds specifically to the neurotoxin saxitoxin. Its physiological role may be to transport or sequester an endogenous organic molecule other than Fe(3+). It may participate in a detoxification mechanism for neutralizing a microbial toxin.
Publication Abstract from PubMed
Dinoflagelates and cyanobacteria produce saxitoxin (STX), a lethal bis-guanidinium neurotoxin causing paralytic shellfish poisoning. A number of metazoans have soluble STX-binding proteins that may prevent STX intoxication. However, their STX molecular recognition mechanisms remain unknown. Here, we present structures of saxiphilin (Sxph), a bullfrog high-affinity STX-binding protein, alone and bound to STX. The structures reveal a novel high-affinity STX-binding site built from a "proto-pocket" on a transferrin scaffold that also bears thyroglobulin domain protease inhibitor repeats. Comparison of Sxph and voltage-gated sodium channel STX-binding sites reveals a convergent toxin recognition strategy comprising a largely rigid binding site where acidic side chains and a cation-pi interaction engage STX. These studies reveal molecular rules for STX recognition, outline how a toxin-binding site can be built on a naive scaffold, and open a path to developing protein sensors for environmental STX monitoring and new biologics for STX intoxication mitigation.
Structure of the saxiphilin:saxitoxin (STX) complex reveals a convergent molecular recognition strategy for paralytic toxins.,Yen TJ, Lolicato M, Thomas-Tran R, Du Bois J, Minor DL Jr Sci Adv. 2019 Jun 19;5(6):eaax2650. doi: 10.1126/sciadv.aax2650. eCollection 2019, Jun. PMID:31223657[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yen TJ, Lolicato M, Thomas-Tran R, Du Bois J, Minor DL Jr. Structure of the saxiphilin:saxitoxin (STX) complex reveals a convergent molecular recognition strategy for paralytic toxins. Sci Adv. 2019 Jun 19;5(6):eaax2650. doi: 10.1126/sciadv.aax2650. eCollection 2019, Jun. PMID:31223657 doi:http://dx.doi.org/10.1126/sciadv.aax2650
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