2bc3: Difference between revisions
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==T7-tagged full-length streptavidin== | ==T7-tagged full-length streptavidin== | ||
<StructureSection load='2bc3' size='340' side='right' caption='[[2bc3]], [[Resolution|resolution]] 1.54Å' scene=''> | <StructureSection load='2bc3' size='340' side='right'caption='[[2bc3]], [[Resolution|resolution]] 1.54Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bc3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1583 As 4.1583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BC3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2bc3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1583 As 4.1583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BC3 FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Avidin|Avidin]] | *[[Avidin 3D structures|Avidin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: As 4 1583]] | [[Category: As 4 1583]] | ||
[[Category: Large Structures]] | |||
[[Category: Humbert, N]] | [[Category: Humbert, N]] | ||
[[Category: Stenkamp, R E]] | [[Category: Stenkamp, R E]] | ||
Revision as of 10:58, 19 February 2020
T7-tagged full-length streptavidinT7-tagged full-length streptavidin
Structural highlights
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 PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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