5b5g: Difference between revisions
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==Crystal structure of ALiS4-Streptavidin complex== | ||
<StructureSection load='5b5g' size='340' side='right'caption='[[5b5g]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5b5g]] 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=5B5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B5G 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]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6FX:METHYL+5-(4-OXIDANYLIDENE-5~{H}-FURO[3,2-C]PYRIDIN-2-YL)PYRIDINE-3-CARBOXYLATE'>6FX</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</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=5b5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b5g OCA], [https://pdbe.org/5b5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b5g RCSB], [https://www.ebi.ac.uk/pdbsum/5b5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b5g 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 == | |||
Chemical inducers that can control target-protein localization in living cells are powerful tools to investigate dynamic biological systems. We recently reported the retention using selective hook or "RUSH" system for reversible localization change of proteins of interest by addition/washout of small-molecule artificial ligands of streptavidin (ALiS). However, the utility of previously developed ALiS was restricted by limited solubility in water. Here, we overcame this problem by X-ray crystal structure-guided design of a more soluble ALiS derivative (ALiS-3), which retains sufficient streptavidin-binding affinity for use in the RUSH system. The ALiS-3-streptavidin interaction was characterized in detail. ALiS-3 is a convenient and effective tool for dynamic control of alpha-mannosidase II localization between ER and Golgi in living cells. | |||
Improving the Solubility of Artificial Ligands of Streptavidin to Enable More Practical Reversible Switching of Protein Localization in Cells.,Tachibana R, Terai T, Boncompain G, Sugiyama S, Saito N, Perez F, Urano Y Chembiochem. 2017 Feb 16;18(4):358-362. doi: 10.1002/cbic.201600640. Epub 2017, Jan 3. PMID:27905160<ref>PMID:27905160</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5b5g" style="background-color:#fffaf0;"></div> | ||
[[Category: Kakinouchi | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Avidin 3D structures|Avidin 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces avidinii]] | |||
[[Category: Fujikake R]] | |||
[[Category: Kakinouchi K]] | |||
[[Category: Nagano T]] | |||
[[Category: Sugiyama S]] | |||
[[Category: Terai T]] | |||
[[Category: Urano Y]] | |||
Latest revision as of 19:00, 8 November 2023
Crystal structure of ALiS4-Streptavidin complexCrystal structure of ALiS4-Streptavidin complex
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 PubMedChemical inducers that can control target-protein localization in living cells are powerful tools to investigate dynamic biological systems. We recently reported the retention using selective hook or "RUSH" system for reversible localization change of proteins of interest by addition/washout of small-molecule artificial ligands of streptavidin (ALiS). However, the utility of previously developed ALiS was restricted by limited solubility in water. Here, we overcame this problem by X-ray crystal structure-guided design of a more soluble ALiS derivative (ALiS-3), which retains sufficient streptavidin-binding affinity for use in the RUSH system. The ALiS-3-streptavidin interaction was characterized in detail. ALiS-3 is a convenient and effective tool for dynamic control of alpha-mannosidase II localization between ER and Golgi in living cells. Improving the Solubility of Artificial Ligands of Streptavidin to Enable More Practical Reversible Switching of Protein Localization in Cells.,Tachibana R, Terai T, Boncompain G, Sugiyama S, Saito N, Perez F, Urano Y Chembiochem. 2017 Feb 16;18(4):358-362. doi: 10.1002/cbic.201600640. Epub 2017, Jan 3. PMID:27905160[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||