Streptavidin Binding Site

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(new page with a simple, quick to load, model of a single subunit)
Current revision (09:23, 1 January 2015) (edit) (undo)
 
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==Streptavidin binds biotin with extraordinary affinity==
==Streptavidin binds biotin with extraordinary affinity==
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<StructureSection load='' size='340' side='right' caption='Biotin' scene='54/547133/Biotin_bs/1'>
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<StructureSection load='' size='340' side='right' caption='Biotin, bound to streptavidin' scene='58/580641/Biotin_bs/1'>
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'''Streptavidin''', from the bacteria ''Streptomyces avidinii'', is a tetrameric protein that has a strong affinity for binding '''biotin''' (the 3D structure of <scene name='58/580641/Biotin_bs/1'>biotin</scene> is now displayed at the right-hand panel).
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{|
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|[[Image:Biotin structure.png]]
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|align="center"| Biotin
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|[[Image:Biotin 3D balls.png]]
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|}
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Streptavidin, from the bacteria ''Streptomyces avidinii'', is a tetrameric protein that has a strong affinity for binding '''biotin''' (the structure of <scene name='54/547133/Biotin_bs/1'>biotin</scene> is now displayed at the right-hand panel).
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You can read more details at the [[Streptavidin|avidin and streptavidin page]]
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You can read more details at [[Streptavidin|Proteopedia's avidin and streptavidin page]]
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This page focuses on the binding site for biotin and how two of the subunits collaborate in binding.
This page focuses on the binding site for biotin and how two of the subunits collaborate in binding.
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The <scene name='54/547133/One_subunit/1'>first display</scene> shows a single subunit of streptavidin with its bound biotin.
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The <scene name='58/580641/One_subunit/1'>first display</scene> shows a single subunit of streptavidin with its bound biotin.
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What does the binding site look like? Let's display the <scene name='54/547133/One_subunit_solid/1'>solid volume of the protein</scene> (in pale blue).
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What does the binding site look like? Let's display the <scene name='58/580641/One_subunit_solid/1'>solid volume of the protein</scene> (in pale blue).
As you see, biotin is embedded inside streptavidin, but a considerable &ndash;and hydrophobic&ndash; part of the biotin molecule remains exposed.
As you see, biotin is embedded inside streptavidin, but a considerable &ndash;and hydrophobic&ndash; part of the biotin molecule remains exposed.
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However, when we add the <scene name='54/547133/One_subunit_solid_solidcover/1'>portion of the neighbouring streptavidin subunit</scene> (residues 116 to 121) that contacts with the first subunit, you will see that it covers most of the biotin molecule.
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However, when we add the <scene name='58/580641/One_subunit_solid_solidcover/1'>portion of the neighbouring streptavidin subunit</scene> (residues 116 to 121) that contacts with the first subunit, you will see that it covers most of the biotin molecule.
Now only the carboxylate group of biotin (note the two red oxygens) sticks out.
Now only the carboxylate group of biotin (note the two red oxygens) sticks out.

Current revision

Streptavidin binds biotin with extraordinary affinity

Biotin, bound to streptavidin

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Angel Herraez, Michal Harel

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