View source for 3wyp


==Crystal structure of wild-type core streptavidin in complex with D-biotin/biotin-D-sulfoxide at 1.3 A resolution==
<StructureSection load='3wyp' size='340' side='right'caption='[[3wyp]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wyp]] is a 4 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=3WYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WYP 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]] 1.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BSO:BIOTIN-D-SULFOXIDE'>BSO</scene>, <scene name='pdbligand=BTN:BIOTIN'>BTN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=3wyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wyp OCA], [https://pdbe.org/3wyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wyp RCSB], [https://www.ebi.ac.uk/pdbsum/3wyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wyp ProSAT]</span></td></tr>
</table>
== 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;">
== Publication Abstract from PubMed ==
We previously created a low-immunogenic core streptavidin mutant No. 314 (LISA-314) by replacing six amino-acid residues for use as a delivery tool for an antibody multistep pre-targeting process (Yumura et al., Protein science, 22, 213-221, 2013). Here, we performed high-resolution X-ray structural analyses of LISA-314 and wild-type streptavidin to investigate the effect of substitutions on the protein function and the three-dimensional structure. LISA-314 forms a tetramer in the same manner as wild-type streptavidin. The binding mode of d-biotin in LISA-314 is also completely identical to that in wild-type streptavidin, and conformational changes were observed mostly at the side chains of substituted sites. Any large conformational changes corresponding to the reduction of B factors around the substituted sites were not observed. These results demonstrated the LISA-314 acquired low immunogenicity without losing structural properties of original wild-type streptavidin.

Crystal structure of streptavidin mutant with low immunogenicity.,Kawato T, Mizohata E, Meshizuka T, Doi H, Kawamura T, Matsumura H, Yumura K, Tsumoto K, Kodama T, Inoue T, Sugiyama A J Biosci Bioeng. 2014 Nov 26. pii: S1389-1723(14)00403-4. doi:, 10.1016/j.jbiosc.2014.10.025. PMID:25434833<ref>PMID:25434833</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wyp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Avidin 3D structures|Avidin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces avidinii]]
[[Category: Doi H]]
[[Category: Inoue T]]
[[Category: Kawamura T]]
[[Category: Kawato T]]
[[Category: Kodama T]]
[[Category: Matsumura H]]
[[Category: Meshizuka T]]
[[Category: Mizohata E]]
[[Category: Sugiyama A]]
[[Category: Tsumoto K]]
[[Category: Yumura K]]