3ry2

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Current revision (12:39, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3ry2' size='340' side='right'caption='[[3ry2]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
<StructureSection load='3ry2' size='340' side='right'caption='[[3ry2]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ry2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/As_4.1583 As 4.1583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RY2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ry2]] 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=3RY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RY2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 0.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ry1|3ry1]]</div></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=BTN:BIOTIN'>BTN</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=3ry2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ry2 OCA], [https://pdbe.org/3ry2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ry2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ry2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ry2 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=3ry2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ry2 OCA], [https://pdbe.org/3ry2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ry2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ry2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ry2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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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[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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Atomic resolution crystallographic studies of streptavidin and its biotin complex have been carried out at 1.03 and 0.95 A, respectively. The wild-type protein crystallized with a tetramer in the asymmetric unit, while the crystals of the biotin complex contained two subunits in the asymmetric unit. Comparison of the six subunits shows the various ways in which the protein accommodates ligand binding and different crystal-packing environments. Conformational variation is found in each of the polypeptide loops connecting the eight strands in the beta-sandwich subunit, but the largest differences are found in the flexible binding loop (residues 45-52). In three of the unliganded subunits the loop is in an `open' conformation, while in the two subunits binding biotin, as well as in one of the unliganded subunits, this loop `closes' over the biotin-binding site. The `closed' loop contributes to the protein's high affinity for biotin. Analysis of the anisotropic displacement parameters included in the crystallographic models is consistent with the variation found in the loop structures and the view that the dynamic nature of the protein structure contributes to the ability of the protein to bind biotin so tightly.
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Streptavidin and its biotin complex at atomic resolution.,Le Trong I, Wang Z, Hyre DE, Lybrand TP, Stayton PS, Stenkamp RE Acta Crystallogr D Biol Crystallogr. 2011 Sep;67(Pt 9):813-21. doi:, 10.1107/S0907444911027806. Epub 2011 Aug 9. PMID:21904034<ref>PMID:21904034</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 3ry2" style="background-color:#fffaf0;"></div>
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==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>
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[[Category: As 4 1583]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lybrand, T P]]
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[[Category: Streptomyces avidinii]]
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[[Category: Stayton, P S]]
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[[Category: Le Trong I]]
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[[Category: Stenkamp, R E]]
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[[Category: Lybrand TP]]
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[[Category: Trong, I Le]]
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[[Category: Stayton PS]]
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[[Category: Biotin]]
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[[Category: Stenkamp RE]]
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[[Category: Biotin-binding protein]]
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Current revision

Wild-type core streptavidin-biotin complex at atomic resolution

PDB ID 3ry2

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Proteopedia Page Contributors and Editors (what is this?)

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