View source for 6o0f


==Saxiphilin:STX complex, co-crystal==
<StructureSection load='6o0f' size='340' side='right'caption='[[6o0f]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6o0f]] 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=6O0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O0F 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]] 2.12&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9SL:[(3aS,4R,10aS)-2,6-diamino-10,10-dihydroxy-3a,4,9,10-tetrahydro-3H,8H-pyrrolo[1,2-c]purin-4-yl]methyl+carbamate'>9SL</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=6o0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o0f OCA], [https://pdbe.org/6o0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o0f RCSB], [https://www.ebi.ac.uk/pdbsum/6o0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o0f ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== 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<ref>PMID:31223657</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6o0f" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lithobates catesbeianus]]
[[Category: Lolicato M]]
[[Category: Minor DL]]
[[Category: Yen TJ]]