4jo6: Difference between revisions
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==Streptavidin complex with SBP-Tag== | ==Streptavidin complex with SBP-Tag== | ||
<StructureSection load='4jo6' size='340' side='right' caption='[[4jo6]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='4jo6' size='340' side='right'caption='[[4jo6]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jo6]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jo6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JO6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jo6 OCA], [https://pdbe.org/4jo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jo6 RCSB], [https://www.ebi.ac.uk/pdbsum/4jo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jo6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 17: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4jo6" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Avidin|Avidin]] | *[[Avidin 3D structures|Avidin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Streptomyces avidinii]] | [[Category: Streptomyces avidinii]] | ||
[[Category: Barrette-Ng | [[Category: Barrette-Ng IH]] | ||
[[Category: Ng | [[Category: Ng KKS]] | ||
[[Category: Tjia | [[Category: Tjia WM]] | ||
[[Category: Wong | [[Category: Wong SL]] | ||
[[Category: Wu | [[Category: Wu SC]] | ||
Latest revision as of 17:24, 8 November 2023
Streptavidin complex with SBP-TagStreptavidin complex with SBP-Tag
Structural highlights
FunctionSAV_STRAV The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMedThe 38-residue SBP-Tag binds to streptavidin more tightly (K(d) -/= 2.5-4.9 nM) than most if not all other known peptide sequences. Crystallographic analysis at 1.75 A resolution shows that the SBP-Tag binds to streptavidin in an unprecedented manner by simultaneously interacting with biotin-binding pockets from two separate subunits. An N-terminal HVV peptide sequence (residues 12-14) and a C-terminal HPQ sequence (residues 31-33) form the bulk of the direct interactions between the SBP-Tag and the two biotin-binding pockets. Surprisingly, most of the peptide spanning these two sites (residues 17-28) adopts a regular alpha-helical structure that projects three leucine side chains into a groove formed at the interface between two streptavidin protomers. The crystal structure shows that residues 1-10 and 35-38 of the original SBP-Tag identified through in vitro selection and deletion analysis do not appear to contact streptavidin and thus may not be important for binding. A 25-residue peptide comprising residues 11-34 (SBP-Tag2) was synthesized and shown using surface plasmon resonance to bind streptavidin with very similar affinity and kinetics when compared with the SBP-Tag. The SBP-Tag2 was also added to the C-terminus of beta-lactamase and was shown to be just as effective as the full-length SBP-Tag in affinity purification. These results validate the molecular structure of the SBP-Tag-streptavidin complex and establish a minimal bivalent streptavidin-binding tag from which further rational design and optimization can proceed. The structure of the SBP-Tag-streptavidin complex reveals a novel helical scaffold bridging binding pockets on separate subunits.,Barrette-Ng IH, Wu SC, Tjia WM, Wong SL, Ng KK Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):879-87. doi:, 10.1107/S0907444913002576. Epub 2013 Apr 19. PMID:23633599[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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