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3t6f

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==Biotin complex of Y54F core streptavidin==
==Biotin complex of Y54F core streptavidin==
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<StructureSection load='3t6f' size='340' side='right' caption='[[3t6f]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
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<StructureSection load='3t6f' size='340' side='right'caption='[[3t6f]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3t6f]] is a 2 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=3T6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T6F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3t6f]] 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=3T6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T6F FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.22&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t6l|3t6l]]</td></tr>
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<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>
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<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=3t6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t6f RCSB], [http://www.ebi.ac.uk/pdbsum/3t6f PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6f OCA], [https://pdbe.org/3t6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t6f RCSB], [https://www.ebi.ac.uk/pdbsum/3t6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t6f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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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[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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We report a point mutation in the second contact shell of the high-affinity streptavidin-biotin complex that appears to reduce binding affinity through transmitted effects on equilibrium dynamics. The Y54F streptavidin mutation causes a 75-fold loss of binding affinity with 73-fold faster dissociation, a large loss of binding enthalpy (DeltaDeltaH, 3.4 kcal/mol at 37 masculineC) and a small gain in binding entropy (TDeltaDeltaS, 0.7 kcal/mol). The removed Y54 hydroxyl is replaced by a water molecule in the bound structure, but there are no observable changes in structure in the first contact shell and no additional changes surrounding the mutation. Molecular dynamics simulations reveal a large increase in atomic fluctuations for W79, a key biotin contact residue, compared to the wild type complex. The increased W79 fluctuations are caused by loss of water-mediated hydrogen bonds between the Y54 hydroxyl group and peptide backbone atoms in and near W79. We propose that the increased fluctuations diminish the integrity of the W79-biotin interaction and represent a loosening of the "tryptophan collar" which is critical to the slow dissociation and high affinity of streptavidin-biotin binding. These results illustrate how changes in protein dynamics distal to the ligand binding pocket can have a profound impact on ligand binding, even when equilibrium structure is unperturbed.
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Second Contact Shell Mutation Diminishes Streptavidin-Biotin Binding Affinity Through Transmitted Effects on Equilibrium Dynamics.,Baugh L, Le Trong I, Cerutti DS, Mehta N, Gulich S, Stayton PS, Stenkamp RE, Lybrand TP Biochemistry. 2011 Dec 6. PMID:22145986<ref>PMID:22145986</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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==See Also==
==See Also==
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*[[Avidin|Avidin]]
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*[[Avidin 3D structures|Avidin 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptomyces avidinii]]
[[Category: Streptomyces avidinii]]
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[[Category: Baugh, L]]
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[[Category: Baugh L]]
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[[Category: Cerutti, D S]]
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[[Category: Cerutti DS]]
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[[Category: Gulich, S]]
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[[Category: Gulich S]]
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[[Category: Lybrand, T P]]
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[[Category: Le Trong I]]
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[[Category: Mehta, N]]
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[[Category: Lybrand TP]]
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[[Category: Stayton, P S]]
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[[Category: Mehta N]]
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[[Category: Stenkamp, R E]]
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[[Category: Stayton PS]]
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[[Category: Trong, I Le]]
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[[Category: Stenkamp RE]]
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[[Category: Biotin binding protein]]
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Current revision

Biotin complex of Y54F core streptavidin

PDB ID 3t6f

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