2bc3: Difference between revisions

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New page: left|200px<br /><applet load="2bc3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bc3, resolution 1.54Å" /> '''T7-tagged full-lengt...
 
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[[Image:2bc3.gif|left|200px]]<br /><applet load="2bc3" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2bc3.gif|left|200px]]<br /><applet load="2bc3" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2bc3, resolution 1.54&Aring;" />
caption="2bc3, resolution 1.54&Aring;" />
'''T7-tagged full-length streptavidin'''<br />
'''T7-tagged full-length streptavidin'''<br />


==Overview==
==Overview==
The structure of a full-length streptavidin has been determined at 1.7 A, resolution and shows that the 20 residue extension at the C terminus forms, a well-ordered polypeptide loop on the surface of the tetramer. Residues, 150-153 of the extension are bound to the ligand-binding site, possibly, competing with exogenous ligands. The binding mode of these residues is, compared with that of biotin and peptidic ligands. The observed structure, helps to rationalize the observations that full-length mature streptavidin, binds biotinylated macromolecules with reduced affinity.
The structure of a full-length streptavidin has been determined at 1.7 A resolution and shows that the 20 residue extension at the C terminus forms a well-ordered polypeptide loop on the surface of the tetramer. Residues 150-153 of the extension are bound to the ligand-binding site, possibly competing with exogenous ligands. The binding mode of these residues is compared with that of biotin and peptidic ligands. The observed structure helps to rationalize the observations that full-length mature streptavidin binds biotinylated macromolecules with reduced affinity.


==About this Structure==
==About this Structure==
2BC3 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 SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BC3 OCA].  
2BC3 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 <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BC3 OCA].  


==Reference==
==Reference==
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[[Category: Streptomyces avidinii]]
[[Category: Streptomyces avidinii]]
[[Category: Humbert, N.]]
[[Category: Humbert, N.]]
[[Category: Stenkamp, R.E.]]
[[Category: Stenkamp, R E.]]
[[Category: Trong, I.Le.]]
[[Category: Trong, I Le.]]
[[Category: Ward, T.R.]]
[[Category: Ward, T R.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: t7 tag]]
[[Category: t7 tag]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:42:49 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:18 2008''

Revision as of 17:36, 21 February 2008

File:2bc3.gif


2bc3, resolution 1.54Å

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T7-tagged full-length streptavidin

OverviewOverview

The structure of a full-length streptavidin has been determined at 1.7 A resolution and shows that the 20 residue extension at the C terminus forms a well-ordered polypeptide loop on the surface of the tetramer. Residues 150-153 of the extension are bound to the ligand-binding site, possibly competing with exogenous ligands. The binding mode of these residues is compared with that of biotin and peptidic ligands. The observed structure helps to rationalize the observations that full-length mature streptavidin binds biotinylated macromolecules with reduced affinity.

About this StructureAbout this Structure

2BC3 is a Single protein structure of sequence from Streptomyces avidinii with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic analysis of a full-length streptavidin with its C-terminal polypeptide bound in the biotin binding site., Le Trong I, Humbert N, Ward TR, Stenkamp RE, J Mol Biol. 2006 Feb 24;356(3):738-45. Epub 2005 Dec 15. PMID:16384581

Page seeded by OCA on Thu Feb 21 16:36:18 2008

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