1rsu

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[[Image:1rsu.gif|left|200px]]
 
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==COMPLEX BETWEEN STREPTAVIDIN AND THE STREP-TAG II PEPTIDE==
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The line below this paragraph, containing "STRUCTURE_1rsu", creates the "Structure Box" on the page.
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<StructureSection load='1rsu' size='340' side='right'caption='[[1rsu]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1rsu]] 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=1RSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RSU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.7&#8491;</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=1rsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsu OCA], [https://pdbe.org/1rsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rsu RCSB], [https://www.ebi.ac.uk/pdbsum/1rsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rsu ProSAT]</span></td></tr>
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{{STRUCTURE_1rsu| PDB=1rsu | SCENE= }}
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</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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rs/1rsu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1rsu ConSurf].
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<div style="clear:both"></div>
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'''COMPLEX BETWEEN STREPTAVIDIN AND THE STREP-TAG II PEPTIDE'''
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==See Also==
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*[[Avidin 3D structures|Avidin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The Strep-tag is a selected nine-amino acid peptide (AWRHPQFGG) that displays intrinsic binding affinity towards streptavidin and has been used as an affinity tag for recombinant proteins. In order to elucidate the molecular mechanism underlying this type of artificial protein-peptide recognition, X-ray crystallographic analyses and binding measurements were carried out. The crystal structure of the complex between recombinant core streptavidin and the synthesized peptide was solved and refined at 1.7 A resolution (space group I4(1)22; unit cell dimensions a = b = 58.3 A, c = 176.9 A). The Strep-tag was bound at the same surface pocket where biotin, the natural ligand of streptavidin, gets complexed. The peptide backbone exhibited 3(10)-helical conformation, with eight of the residues involved in protein contacts. The C-terminal Gly-Gly moiety of the Strep-tag participated in a salt bridge to Arg84 of streptavidin with its free carboxylate group. This finding explained why the use of the Strep-tag in fusions with recombinant proteins was restricted to their carboxyl end. Employing a synthetic peptide spot assay, the variant Strep-tag II was screened, which did not have this limitation. The isomorphous crystal structure of its complex with streptavidin revealed that a glutamate side-chain provided the salt bridge in this case, with an otherwise almost unchanged mode of binding. Affinity constants between the peptides and streptavidin were measured by isothermal titration calorimetry. A value of 2.7 x 10(4) M-1 was determined for the Strep-tag peptide, and slightly tighter binding was seen when the Strep-tag was applied as part of a bacterially produced fusion protein. This affinity is significantly higher, compared with values previously reported for shorter streptavidin-binding peptides, and agrees well with the remarkable selectivity observed in recombinant protein purification applications.
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[[Category: Large Structures]]
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==About this Structure==
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1RSU is a [[Single protein]] structure of 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=1RSU OCA].
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==Reference==
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Molecular interaction between the Strep-tag affinity peptide and its cognate target, streptavidin., Schmidt TG, Koepke J, Frank R, Skerra A, J Mol Biol. 1996 Feb 9;255(5):753-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8636976 8636976]
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[[Category: Single protein]]
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[[Category: Streptomyces avidinii]]
[[Category: Streptomyces avidinii]]
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[[Category: Koepke, J.]]
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[[Category: Koepke J]]
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[[Category: Schmidt, T.]]
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[[Category: Schmidt T]]
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[[Category: Skerra, A.]]
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[[Category: Skerra A]]
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[[Category: Signal protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:51:51 2008''
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COMPLEX BETWEEN STREPTAVIDIN AND THE STREP-TAG II PEPTIDE

PDB ID 1rsu

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