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[[Image:1vyo.gif|left|200px]]<br />
<applet load="1vyo" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1vyo, resolution 1.48&Aring;" />
'''CRYSTAL STRUCTURE OF AVIDIN'''<br />


==Overview==
==Crystal structure of avidin==
The chicken genome encodes several biotin-binding proteins, including, avidin and avidin-related protein 4 (AVR4). In addition to D-biotin, avidin binds an azo dye compound, 4-hydroxyazobenzene-2-carboxylic acid, (HABA), but the HABA-binding properties of AVR4 are not yet known., Differential scanning calorimetry, UV/visible spectroscopy, and molecular, modeling were used to analyze the binding of 15 azo molecules to avidin, and AVR4. Significant differences are seen in azo compound preferences for, the two proteins, emphasizing the importance of the loop between strands, beta3 and beta4 for azo ligand recognition; information on these loops is, provided by the high-resolution (1.5 A) X-ray structure for avidin, reported here. These results may be valuable in designing improved tools, for ... [[http://ispc.weizmann.ac.il/pmbin/getpm?17052607 (full description)]]
<StructureSection load='1vyo' size='340' side='right'caption='[[1vyo]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vyo]] 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=1VYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VYO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48&#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></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=1vyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vyo OCA], [https://pdbe.org/1vyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vyo RCSB], [https://www.ebi.ac.uk/pdbsum/1vyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vyo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AVID_CHICK AVID_CHICK] The biological function of avidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of avidin).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vy/1vyo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1vyo ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The chicken genome encodes several biotin-binding proteins, including avidin and avidin-related protein 4 (AVR4). In addition to D-biotin, avidin binds an azo dye compound, 4-hydroxyazobenzene-2-carboxylic acid (HABA), but the HABA-binding properties of AVR4 are not yet known. Differential scanning calorimetry, UV/visible spectroscopy, and molecular modeling were used to analyze the binding of 15 azo molecules to avidin and AVR4. Significant differences are seen in azo compound preferences for the two proteins, emphasizing the importance of the loop between strands beta3 and beta4 for azo ligand recognition; information on these loops is provided by the high-resolution (1.5 A) X-ray structure for avidin reported here. These results may be valuable in designing improved tools for avidin-based life science and nanobiotechnology applications.


==About this Structure==
Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4.,Repo S, Paldanius TA, Hytonen VP, Nyholm TK, Halling KK, Huuskonen J, Pentikainen OT, Rissanen K, Slotte JP, Airenne TT, Salminen TA, Kulomaa MS, Johnson MS Chem Biol. 2006 Oct;13(10):1029-39. PMID:17052607<ref>PMID:17052607</ref>
1VYO 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 GOL as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VYO OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4., Repo S, Paldanius TA, Hytonen VP, Nyholm TK, Halling KK, Huuskonen J, Pentikainen OT, Rissanen K, Slotte JP, Airenne TT, Salminen TA, Kulomaa MS, Johnson MS, Chem Biol. 2006 Oct;13(10):1029-39. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17052607 17052607]
</div>
<div class="pdbe-citations 1vyo" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Avidin 3D structures|Avidin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Airenne, T.T.]]
[[Category: Airenne TT]]
[[Category: Johnson, M.S.]]
[[Category: Johnson MS]]
[[Category: Salminen, T.A.]]
[[Category: Salminen TA]]
[[Category: GOL]]
[[Category: biotin]]
[[Category: glycoprotein]]
 
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