3rdm: Difference between revisions
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==Crystal structure of R7-2 streptavidin complexed with biotin/PEG== | ==Crystal structure of R7-2 streptavidin complexed with biotin/PEG== | ||
<StructureSection load='3rdm' size='340' side='right' caption='[[3rdm]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='3rdm' size='340' side='right'caption='[[3rdm]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rdm]] is a 1 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=3RDM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RDM FirstGlance]. <br> | <table><tr><td colspan='2'>[[3rdm]] is a 1 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=3RDM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RDM FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3rdm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3rdm" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[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: Almo, S C]] | [[Category: Almo, S C]] | ||
[[Category: Czecster, C M]] | [[Category: Czecster, C M]] | ||
Revision as of 16:39, 25 December 2019
Crystal structure of R7-2 streptavidin complexed with biotin/PEGCrystal structure of R7-2 streptavidin complexed with biotin/PEG
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). Publication Abstract from PubMedWe have performed a detailed analysis of streptavidin variants with altered specificity towards desthiobiotin. In addition to changes in key residues which widen the ligand binding pocket and accommodate the more structurally flexible desthiobiotin, the data revealed the role of a key, non-active site mutation at the base of the flexible loop (S52G) which slows dissociation of this ligand by approximately sevenfold. Our data suggest that this mutation results in the loss of a stabilizing contact which keeps this loop open and accessible in the absence of ligand. When this mutation was introduced into the wild-type protein, destabilization of the opened loop conferred a approximately 10-fold decrease in both the on-rate and off-rate for the ligand biotin-4-fluoroscein. A similar effect was observed when this mutation was added to a monomeric form of this protein. Our results provide key insight into the role of the streptavidin flexible loop in ligand binding and maintaining high affinity interactions. Evolved streptavidin mutants reveal key role of loop residue in high-affinity binding.,Magalhaes ML, Czekster CM, Guan R, Malashkevich VN, Almo SC, Levy M Protein Sci. 2011 Jul;20(7):1145-54. doi: 10.1002/pro.642. Epub 2011 May, 12. PMID:21520321[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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