6ud6

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Current revision (05:50, 21 November 2024) (edit) (undo)
 
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<StructureSection load='6ud6' size='340' side='right'caption='[[6ud6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='6ud6' size='340' side='right'caption='[[6ud6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ud6]] is a 2 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=6UD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UD6 FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UD6 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]] 1.502&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.502&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DV7:L-(7-hydroxycoumarin-4-yl)ethylglycine'>DV7</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DV7:L-(7-hydroxycoumarin-4-yl)ethylglycine'>DV7</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6ud6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ud6 OCA], [https://pdbe.org/6ud6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ud6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ud6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ud6 ProSAT]</span></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=6ud6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ud6 OCA], [https://pdbe.org/6ud6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ud6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ud6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ud6 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[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).
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Fluorescent noncanonical amino acids (fNCAAs) could serve as starting points for the rational design of protein-based fluorescent sensors of biological activity. However, efforts toward this goal are likely hampered by a lack of atomic-level characterization of fNCAAs within proteins. Here, we describe the spectroscopic and structural characterization of five streptavidin mutants that contain the fNCAA l-(7-hydroxycoumarin-4-yl)ethylglycine (7-HCAA) at sites proximal to the binding site of its substrate, biotin. Many of the mutants exhibited altered fluorescence spectra in response to biotin binding, which included both increases and decreases in fluorescence intensity as well as red- or blue-shifted emission maxima. Structural data were also obtained for three of the five mutants. The crystal structures shed light on interactions between 7-HCAA and functional groups, contributed either by the protein or by the substrate, that may be responsible for the observed changes in the 7-HCAA spectra. These data could be used in future studies aimed at the rational design of fluorescent, protein-based sensors of small molecule binding or dissociation.
 
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Structural Origins of Altered Spectroscopic Properties upon Ligand Binding in Proteins Containing a Fluorescent Noncanonical Amino Acid.,Gleason PR, Kolbaba-Kartchner B, Henderson JN, Stahl EP, Simmons CR, Mills JH Biochemistry. 2021 Aug 31;60(34):2577-2585. doi: 10.1021/acs.biochem.1c00291., Epub 2021 Aug 20. PMID:34415744<ref>PMID:34415744</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 6ud6" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Avidin 3D structures|Avidin 3D structures]]
*[[Avidin 3D structures|Avidin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Streptomyces avidinii]]
 
[[Category: Gleason PR]]
[[Category: Gleason PR]]
[[Category: Henderson JN]]
[[Category: Henderson JN]]

Current revision

Spectroscopic and structural characterization of a genetically encoded direct sensor for protein-ligand interactions

PDB ID 6ud6

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