1lcv: Difference between revisions

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New page: left|200px<br /><applet load="1lcv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lcv, resolution 2.3Å" /> '''streptavidin-norbioti...
 
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[[Image:1lcv.gif|left|200px]]<br /><applet load="1lcv" size="450" color="white" frame="true" align="right" spinBox="true"
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'''streptavidin-norbiotin complex'''<br />


==Overview==
==streptavidin-norbiotin complex==
We have studied the structural elements that affect ligand exchange, between the two high affinity biotin-binding proteins, egg white avidin, and its bacterial analogue, streptavidin. For this purpose, we have, developed a simple assay based on the antipodal behavior of the two, proteins toward hydrolysis of biotinyl p-nitrophenyl ester (BNP). The, assay provided the experimental basis for these studies. It was found that, biotin migrates unidirectionally from streptavidin to avidin. Conversely, the biotin derivative, BNP, is transferred in the opposite direction, from, avidin to streptavidin. A previous crystallographic study (Huberman, T., Eisenberg-Domovich, Y., Gitlin, G., Kulik, T., Bayer, E. A., Wilchek, M., and Livnah, O. (2001) J. Biol. Chem. 276, 32031-32039) provided insight, into a plausible explanation for these results. These data revealed that, the non-hydrolyzable BNP analogue, biotinyl p-nitroanilide, was almost, completely sheltered in streptavidin as opposed to avidin in which the, disordered conformation of a critical loop resulted in the loss of several, hydrogen bonds and concomitant exposure of the analogue to the solvent. In, order to determine the minimal modification of the biotin molecule, required to cause the disordered loop conformation, the structures of, avidin and streptavidin were determined with norbiotin, homobiotin, and a, common long-chain biotin derivative, biotinyl epsilon-aminocaproic acid., Six new crystal structures of the avidin and streptavidin complexes with, the latter biotin analogues and derivatives were thus elucidated. It was, found that extending the biotin side chain by a single CH(2) group (i.e., homobiotin) is sufficient to result in this remarkable conformational, change in the loop of avidin. These results bear significant, biotechnological importance, suggesting that complexes containing, biotinylated probes with streptavidin would be more stable than those with, avidin. These findings should be heeded when developing new drugs based on, lead compounds because it is difficult to predict the structural and, conformational consequences on the resultant protein-ligand interactions.
<StructureSection load='1lcv' size='340' side='right'caption='[[1lcv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lcv]] 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=1LCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LCV 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SNR:NORBIOTIN'>SNR</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=1lcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lcv OCA], [https://pdbe.org/1lcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lcv RCSB], [https://www.ebi.ac.uk/pdbsum/1lcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lcv ProSAT]</span></td></tr>
</table>
== 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).
== 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/lc/1lcv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1lcv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LCV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with SNR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LCV OCA].
*[[Avidin 3D structures|Avidin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Ligand exchange between proteins. Exchange of biotin and biotin derivatives between avidin and streptavidin., Pazy Y, Kulik T, Bayer EA, Wilchek M, Livnah O, J Biol Chem. 2002 Aug 23;277(34):30892-900. Epub 2002 Jun 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12055191 12055191]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Streptomyces avidinii]]
[[Category: Streptomyces avidinii]]
[[Category: Livnah, O.]]
[[Category: Livnah O]]
[[Category: Pazy, Y.]]
[[Category: Pazy Y]]
[[Category: SNR]]
[[Category: avidin]]
[[Category: biotin]]
[[Category: biotin-analogues]]
[[Category: streptavidin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:29:06 2007''

Latest revision as of 10:32, 14 February 2024

streptavidin-norbiotin complexstreptavidin-norbiotin complex

Structural highlights

1lcv 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 2.3Å
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

1lcv, resolution 2.30Å

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