Single stranded binding protein: Difference between revisions
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==Binding Interactions in the Active Site== | ==Binding Interactions in the Active Site== | ||
<scene name='56/566528/Ssdna/1'>Single-stranded DNA</scene> can interact with SSB through hydrogen bonds, stacking, or electrostatic interactions. Though SSB proteins are found in a variety of different organisms, most interactions between SSB and ssDNA happen through the common structural motif of an oligosaccharide/oligonucleotide binding site, referred to as the <scene name='56/566528/Ob_fold/4'>OB fold</scene> <ref>Shamoo, Yousif. “Single Stranded DNA binding proteins.” ‘’Encyclopedia of Life Sciences.’’ MacMillan Publishers Ltd, Nature Publishing Group; 2002</ref>. The OB fold allows SSB to bind preferentially to ssDNA. Each subunit of a SSB has an <scene name='56/566528/Ob_fold/1'>OB fold</scene> (the SSB of E. coli thus has <scene name='56/566528/Ob_fold/2'>four OB folds</scene>, one per each of its <scene name='56/566528/Homotetramer/1'>four identical subunits</scene>). This fold consists of a <scene name='56/566528/Beta_barrel/1'>5 stranded β barrel</scene> that ends in an <scene name='56/566528/Beta_barrel/2'>α-helix</scene>. | <scene name='56/566528/Ssdna/1'>Single-stranded DNA</scene> can interact with SSB through hydrogen bonds, stacking, or electrostatic interactions. Though SSB proteins are found in a variety of different organisms, most interactions between SSB and ssDNA happen through the common structural motif of an oligosaccharide/oligonucleotide binding site, referred to as the <scene name='56/566528/Ob_fold/4'>OB fold</scene> <ref>Shamoo, Yousif. “Single Stranded DNA binding proteins.” ‘’Encyclopedia of Life Sciences.’’ MacMillan Publishers Ltd, Nature Publishing Group; 2002</ref>. The OB fold allows SSB to bind preferentially to ssDNA. Each subunit of a SSB has an <scene name='56/566528/Ob_fold/1'>OB fold</scene> (the SSB of E. coli thus has <scene name='56/566528/Ob_fold/2'>four OB folds</scene>, one per each of its <scene name='56/566528/Homotetramer/1'>four identical subunits</scene>). This fold consists of a <scene name='56/566528/Beta_barrel/1'>5 stranded β barrel</scene> that ends in an <scene name='56/566528/Beta_barrel/2'>α-helix</scene>. | ||