4jo6: Difference between revisions
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==Streptavidin complex with SBP-Tag== | |||
=== | <StructureSection load='4jo6' size='340' side='right' caption='[[4jo6]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jo6]] is a 6 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JO6 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1swe|1swe]]</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=4jo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jo6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jo6 RCSB], [http://www.ebi.ac.uk/pdbsum/4jo6 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:23633599</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[Avidin|Avidin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Streptomyces avidinii]] | [[Category: Streptomyces avidinii]] | ||
[[Category: Barrette-Ng, I H | [[Category: Barrette-Ng, I H]] | ||
[[Category: Ng, K K.S | [[Category: Ng, K K.S]] | ||
[[Category: Tjia, W M | [[Category: Tjia, W M]] | ||
[[Category: Wong, S L | [[Category: Wong, S L]] | ||
[[Category: Wu, S C | [[Category: Wu, S C]] | ||
[[Category: Biotechnological targeting]] | [[Category: Biotechnological targeting]] | ||
[[Category: Biotin and peptide binding]] | [[Category: Biotin and peptide binding]] | ||
[[Category: Homotetramer bound to peptide]] | [[Category: Homotetramer bound to peptide]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] |