Streptavidin Binding Site

From Proteopedia

(Difference between revisions)

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 <StructureSection load='' size='340' side='right' caption='Biotin' scene='54/547133/Biotin_bs/1'>
-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).
+Streptavidin, from the bacteria ''Streptomyces avidinii'', is a tetrameric protein that has a strong affinity for binding '''biotin''' (the structure of <scene name='58/580641/Biotin_bs/1'>biotin</scene> is now displayed at the right-hand panel).
 You can read more details at [[Streptavidin|Proteopedia's avidin and streptavidin page]]
 This page focuses on the binding site for biotin and how two of the subunits collaborate in binding.
-The <scene name='54/547133/One_subunit/1'>first display</scene> shows a single subunit of streptavidin with its bound biotin.
+The <scene name='58/580641/One_subunit/1'>first display</scene> shows a single subunit of streptavidin with its bound biotin.
-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).
+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.
-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.
+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.

Revision as of 09:10, 19 March 2014

Streptavidin binds biotin with extraordinary affinity

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Biotin

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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 is now displayed at the right-hand panel). You can read more details at Proteopedia's avidin and streptavidin page

This page focuses on the binding site for biotin and how two of the subunits collaborate in binding.

The shows a single subunit of streptavidin with its bound biotin.

What does the binding site look like? Let's display the (in pale blue).

As you see, biotin is embedded inside streptavidin, but a considerable –and hydrophobic– part of the biotin molecule remains exposed.

However, when we add the (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.