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[[Image:2f01.gif|left|200px]]
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{{STRUCTURE_2f01|  PDB=2f01  |  SCENE=  }}
'''Epi-biotin complex with core streptavidin'''


==Epi-biotin complex with core streptavidin==
<StructureSection load='2f01' size='340' side='right'caption='[[2f01]], [[Resolution|resolution]] 0.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2f01]] 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=2F01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F01 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]] 0.85&#8491;</td></tr>
<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=BTQ:EPI-BIOTIN'>BTQ</scene>, <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=2f01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f01 OCA], [https://pdbe.org/2f01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f01 RCSB], [https://www.ebi.ac.uk/pdbsum/2f01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f01 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/f0/2f01_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=2f01 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
(+)-Epi-biotin differs from (+)-biotin in the configuration of the chiral center at atom C2. This could lead to a difference in the mode of binding of (+)-epi-biotin to streptavidin, a natural protein receptor for (+)-biotin. Diffraction data were collected to a maximum of 0.85 Angstrom resolution for structural analysis of the complex of streptavidin with a sample of (+)-epi-biotin and refinement was carried out at both 1.0 and 0.85 Angstrom resolution. The structure determination shows a superposition of two ligands in the binding site, (+)-biotin and (+)-epi-biotin. The molecules overlap in the model for the complex except for the position of S1 in the tetrahydrothiophene ring. Differences in the conformation of the ring permits binding of each molecule to streptavidin with little observable difference in the protein structures at this high resolution.


==Overview==
The high-resolution structure of (+)-epi-biotin bound to streptavidin.,Le Trong I, Aubert DG, Thomas NR, Stenkamp RE Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):576-81. Epub 2006, May 12. PMID:16699183<ref>PMID:16699183</ref>
(+)-Epi-biotin differs from (+)-biotin in the configuration of the chiral center at atom C2. This could lead to a difference in the mode of binding of (+)-epi-biotin to streptavidin, a natural protein receptor for (+)-biotin. Diffraction data were collected to a maximum of 0.85 Angstrom resolution for structural analysis of the complex of streptavidin with a sample of (+)-epi-biotin and refinement was carried out at both 1.0 and 0.85 Angstrom resolution. The structure determination shows a superposition of two ligands in the binding site, (+)-biotin and (+)-epi-biotin. The molecules overlap in the model for the complex except for the position of S1 in the tetrahydrothiophene ring. Differences in the conformation of the ring permits binding of each molecule to streptavidin with little observable difference in the protein structures at this high resolution.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2F01 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=2F01 OCA].
</div>
<div class="pdbe-citations 2f01" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The high-resolution structure of (+)-epi-biotin bound to streptavidin., Le Trong I, Aubert DG, Thomas NR, Stenkamp RE, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):576-81. Epub 2006, May 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16699183 16699183]
*[[Avidin 3D structures|Avidin 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces avidinii]]
[[Category: Streptomyces avidinii]]
[[Category: Aubert, D G.]]
[[Category: Aubert DG]]
[[Category: Stenkamp, R E.]]
[[Category: Le Trong I]]
[[Category: Thomas, N R.]]
[[Category: Stenkamp RE]]
[[Category: Trong, I Le.]]
[[Category: Thomas NR]]
[[Category: Biotin]]
[[Category: Protein/ligand interaction]]
[[Category: Streptavidin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:18:05 2008''

Latest revision as of 10:41, 23 August 2023

Epi-biotin complex with core streptavidinEpi-biotin complex with core streptavidin

Structural highlights

2f01 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 0.85Å
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.

Publication Abstract from PubMed

(+)-Epi-biotin differs from (+)-biotin in the configuration of the chiral center at atom C2. This could lead to a difference in the mode of binding of (+)-epi-biotin to streptavidin, a natural protein receptor for (+)-biotin. Diffraction data were collected to a maximum of 0.85 Angstrom resolution for structural analysis of the complex of streptavidin with a sample of (+)-epi-biotin and refinement was carried out at both 1.0 and 0.85 Angstrom resolution. The structure determination shows a superposition of two ligands in the binding site, (+)-biotin and (+)-epi-biotin. The molecules overlap in the model for the complex except for the position of S1 in the tetrahydrothiophene ring. Differences in the conformation of the ring permits binding of each molecule to streptavidin with little observable difference in the protein structures at this high resolution.

The high-resolution structure of (+)-epi-biotin bound to streptavidin.,Le Trong I, Aubert DG, Thomas NR, Stenkamp RE Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):576-81. Epub 2006, May 12. PMID:16699183[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Le Trong I, Aubert DG, Thomas NR, Stenkamp RE. The high-resolution structure of (+)-epi-biotin bound to streptavidin. Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):576-81. Epub 2006, May 12. PMID:16699183 doi:http://dx.doi.org/10.1107/S0907444906011887

2f01, resolution 0.85Å

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