2bc3: Difference between revisions

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<StructureSection load='2bc3' size='340' side='right'caption='[[2bc3]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
<StructureSection load='2bc3' size='340' side='right'caption='[[2bc3]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2bc3]] 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=2BC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BC3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2bc3]] 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=2BC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BC3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.54&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2bc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bc3 OCA], [https://pdbe.org/2bc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bc3 RCSB], [https://www.ebi.ac.uk/pdbsum/2bc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bc3 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=2bc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bc3 OCA], [https://pdbe.org/2bc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bc3 RCSB], [https://www.ebi.ac.uk/pdbsum/2bc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bc3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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).  
[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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bc3 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bc3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of a full-length streptavidin has been determined at 1.7 A resolution and shows that the 20 residue extension at the C terminus forms a well-ordered polypeptide loop on the surface of the tetramer. Residues 150-153 of the extension are bound to the ligand-binding site, possibly competing with exogenous ligands. The binding mode of these residues is compared with that of biotin and peptidic ligands. The observed structure helps to rationalize the observations that full-length mature streptavidin binds biotinylated macromolecules with reduced affinity.
Crystallographic analysis of a full-length streptavidin with its C-terminal polypeptide bound in the biotin binding site.,Le Trong I, Humbert N, Ward TR, Stenkamp RE J Mol Biol. 2006 Feb 24;356(3):738-45. Epub 2005 Dec 15. PMID:16384581<ref>PMID:16384581</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2bc3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Avidin 3D structures|Avidin 3D structures]]
*[[Avidin 3D structures|Avidin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: As 4 1583]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Humbert, N]]
[[Category: Streptomyces avidinii]]
[[Category: Stenkamp, R E]]
[[Category: Humbert N]]
[[Category: Trong, I Le]]
[[Category: Le Trong I]]
[[Category: Ward, T R]]
[[Category: Stenkamp RE]]
[[Category: Biotin binding protein]]
[[Category: Ward TR]]
[[Category: Streptavidin]]
[[Category: T7 tag]]

Latest revision as of 09:24, 3 April 2024

T7-tagged full-length streptavidinT7-tagged full-length streptavidin

Structural highlights

2bc3 is a 2 chain structure with sequence from Streptomyces avidinii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.54Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2bc3, resolution 1.54Å

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