1rxk

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[[Image:1rxk.gif|left|200px]]
 
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==crystal structure of streptavidin mutant (M3) a combination of M1+M2==
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The line below this paragraph, containing "STRUCTURE_1rxk", creates the "Structure Box" on the page.
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<StructureSection load='1rxk' size='340' side='right'caption='[[1rxk]], [[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'>[[1rxk]] 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=1RXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RXK 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNI:5-(2-OXO-HEXAHYDRO-THIENO[3,4-D]IMIDAZOL-6-YL)-PENTANOIC+ACID+(4-NITRO-PHENYL)-AMIDE'>BNI</scene></td></tr>
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{{STRUCTURE_1rxk| PDB=1rxk | SCENE= }}
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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=1rxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxk OCA], [https://pdbe.org/1rxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rxk RCSB], [https://www.ebi.ac.uk/pdbsum/1rxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxk ProSAT]</span></td></tr>
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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/rx/1rxk_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=1rxk ConSurf].
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<div style="clear:both"></div>
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'''crystal structure of streptavidin mutant (M3) a combination of M1+M2'''
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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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Avidin enhances the hydrolysis of biotinyl p-nitrophenyl ester (BNP) under mild alkaline conditions, whereas streptavidin prevents hydrolysis of BNP up to pH 12. Recently, we imposed hydrolytic activity on streptavidin by rational mutagenesis, based on the molecular elements responsible for the hydrolysis by avidin. Three mutants were designed, whereby the desired features, the distinctive L124R point mutation (M1), the L3,4 loop replacement (M2), and the combined mutation (M3), were transferred from avidin to streptavidin. The crystal structures of the mutants, in complex with biotinyl p-nitroanilide (BNA), the stable amide analogue of BNP, were determined. The results demonstrate that the point mutation alone has little effect on hydrolysis, and BNA exhibits a conformation similar to that of streptavidin. Substitution of a lengthier L3,4 loop (from avidin to streptavidin), resulted in an open conformation, thus exposing the ligand to solvent. Moreover, the amide bond of BNA was flipped relative to that of the streptavidin and M1 complexes, thus deflecting the nitro group toward Lys-121. Consequently, the leaving group potential of the nitrophenyl group of BNP is increased, and M2 hydrolyzes BNP at pH values &gt;8.5. To better emulate the hydrolytic potential of avidin, M3 was required. The combination of loop replacement and point mutation served to further increase the leaving group potential by interaction of the nitro group with Arg-124 and Lys-121. The information derived from this study may provide insight into the design of enzymes and transfer of desired properties among homologous proteins.
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[[Category: Large Structures]]
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==About this Structure==
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1RXK 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=1RXK OCA].
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==Reference==
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Structural elements responsible for conversion of streptavidin to a pseudoenzyme., Eisenberg-Domovich Y, Pazy Y, Nir O, Raboy B, Bayer EA, Wilchek M, Livnah O, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5916-21. Epub 2004 Apr 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15079055 15079055]
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[[Category: Single protein]]
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[[Category: Streptomyces avidinii]]
[[Category: Streptomyces avidinii]]
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[[Category: Bayer, E A.]]
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[[Category: Bayer EA]]
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[[Category: Eisenberg-Domovich, Y.]]
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[[Category: Eisenberg-Domovich Y]]
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[[Category: Livnah, O.]]
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[[Category: Livnah O]]
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[[Category: Nir, O.]]
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[[Category: Nir O]]
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[[Category: Pazy, Y.]]
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[[Category: Pazy Y]]
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[[Category: Raboy, B.]]
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[[Category: Raboy B]]
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[[Category: Wilchek, M.]]
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[[Category: Wilchek M]]
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[[Category: Avidin]]
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[[Category: Pseudo enzymatic activity]]
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[[Category: Streptavidin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:01:45 2008''
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Current revision

crystal structure of streptavidin mutant (M3) a combination of M1+M2

PDB ID 1rxk

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