1y55

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(New page: 200px<br /><applet load="1y55" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y55, resolution 1.00&Aring;" /> '''Crystal structure of...)
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[[Image:1y55.gif|left|200px]]<br /><applet load="1y55" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1y55, resolution 1.00&Aring;" />
 
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'''Crystal structure of the C122S mutant of E. Coli expressed avidin related protein 4 (AVR4)-biotin complex'''<br />
 
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==Overview==
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==Crystal structure of the C122S mutant of E. Coli expressed avidin related protein 4 (AVR4)-biotin complex==
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The chicken avidin gene belongs to an extended gene family encoding seven, avidin-related genes (AVRs), of which only avidin is expressed in the, chicken. The sequences of AVR4 and AVR5 are identical and the common, protein (AVR4) has been expressed both in insect and bacterial systems., The recombinant proteins are similarly hyperthermostable and bind biotin, with similarly high affinities. AVR4 was crystallized in the apo and, biotin-complexed forms and their structures were determined at high, resolution. Its tertiary and quaternary structures are very similar to, those of avidin and streptavidin. Its biotin-binding site shows only a few, alterations compared with those of avidin and streptavidin, which account, for the observed differences in binding affinities. The increased, hyperthermostability can be attributed to the conformation of the critical, L3,4 loop and the extensive network of 1-3 inter-monomeric interactions., The loop contains a tandem Pro-Gly sequence and an Asp-Arg ion pair that, collectively induce rigidity, thus maintaining its closed and ordered, conformation in both the apo and biotin-complexed forms. In addition, Tyr115 is present on the AVR4 1-3 monomer-monomer interface, which is, absent in avidin and streptavidin. The interface tyrosine generates, inter-monomeric interactions, i.e. a tyrosine-tyrosine pi-pi interaction, and a hydrogen bond with Lys92. The resultant network of interactions, confers a larger 1-3 dimer-dimer contact surface on AVR4, which correlates, nicely with its higher thermostability compared with avidin and, streptavidin. Several of the proposed thermostability-determining factors, were found to play a role in strengthening the tertiary and quaternary, integrity of AVR4.
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<StructureSection load='1y55' size='340' side='right'caption='[[1y55]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1y55]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y55 FirstGlance]. <br>
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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&#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=BTN:BIOTIN'>BTN</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></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=1y55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y55 OCA], [https://pdbe.org/1y55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y55 RCSB], [https://www.ebi.ac.uk/pdbsum/1y55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y55 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AVR4_CHICK AVR4_CHICK]
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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/y5/1y55_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1y55 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The chicken avidin gene belongs to an extended gene family encoding seven avidin-related genes (AVRs), of which only avidin is expressed in the chicken. The sequences of AVR4 and AVR5 are identical and the common protein (AVR4) has been expressed both in insect and bacterial systems. The recombinant proteins are similarly hyperthermostable and bind biotin with similarly high affinities. AVR4 was crystallized in the apo and biotin-complexed forms and their structures were determined at high resolution. Its tertiary and quaternary structures are very similar to those of avidin and streptavidin. Its biotin-binding site shows only a few alterations compared with those of avidin and streptavidin, which account for the observed differences in binding affinities. The increased hyperthermostability can be attributed to the conformation of the critical L3,4 loop and the extensive network of 1-3 inter-monomeric interactions. The loop contains a tandem Pro-Gly sequence and an Asp-Arg ion pair that collectively induce rigidity, thus maintaining its closed and ordered conformation in both the apo and biotin-complexed forms. In addition, Tyr115 is present on the AVR4 1-3 monomer-monomer interface, which is absent in avidin and streptavidin. The interface tyrosine generates inter-monomeric interactions, i.e. a tyrosine-tyrosine pi-pi interaction and a hydrogen bond with Lys92. The resultant network of interactions confers a larger 1-3 dimer-dimer contact surface on AVR4, which correlates nicely with its higher thermostability compared with avidin and streptavidin. Several of the proposed thermostability-determining factors were found to play a role in strengthening the tertiary and quaternary integrity of AVR4.
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==About this Structure==
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High-resolution crystal structure of an avidin-related protein: insight into high-affinity biotin binding and protein stability.,Eisenberg-Domovich Y, Hytonen VP, Wilchek M, Bayer EA, Kulomaa MS, Livnah O Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):528-38. Epub 2005, Apr 20. PMID:15858262<ref>PMID:15858262</ref>
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1Y55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with BTN and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y55 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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High-resolution crystal structure of an avidin-related protein: insight into high-affinity biotin binding and protein stability., Eisenberg-Domovich Y, Hytonen VP, Wilchek M, Bayer EA, Kulomaa MS, Livnah O, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):528-38. Epub 2005, Apr 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15858262 15858262]
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</div>
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[[Category: Gallus gallus]]
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<div class="pdbe-citations 1y55" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Bayer, E.A.]]
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[[Category: Eisenberg-Domovich, Y.]]
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[[Category: Hytonen, V.P.]]
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[[Category: Kulomaa, M.S.]]
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[[Category: Livnah, O.]]
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[[Category: Wilchek, M.]]
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[[Category: BTN]]
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[[Category: FMT]]
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[[Category: avidin]]
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[[Category: avidin related molecule]]
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[[Category: biotin]]
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[[Category: high affinity]]
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[[Category: streptavidin]]
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[[Category: thermostability]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:34:34 2007''
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==See Also==
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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__
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</StructureSection>
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[[Category: Gallus gallus]]
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[[Category: Large Structures]]
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[[Category: Bayer EA]]
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[[Category: Eisenberg-Domovich Y]]
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[[Category: Hytonen VP]]
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[[Category: Kulomaa MS]]
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[[Category: Livnah O]]
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[[Category: Wilchek M]]

Current revision

Crystal structure of the C122S mutant of E. Coli expressed avidin related protein 4 (AVR4)-biotin complex

PDB ID 1y55

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