Single stranded binding protein: Difference between revisions
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<StructureSection load='2vw9' size='500' side='right' frame='true' caption='Structure of Single Stranded DNA-Binding Protein bound to ssDNA (PDB entry [[2vw9]])' scene=''> | <StructureSection load='2vw9' size='500' side='right' frame='true' caption='Structure of Single Stranded DNA-Binding Protein bound to ssDNA (PDB entry [[2vw9]])' scene=''> | ||
==Structure== | ==Structure== | ||
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</StructureSection> | </StructureSection> | ||
<StructureSection load='1qvc' size='500' side='right' frame='true' caption='Structure of Single Stranded DNA-Binding Protein from ''E. coli'' (PDB entry [[1qvc]])' scene=''> | |||
==Binding Interactions between DNA and SSB of ''E. coli''== | |||
Phe60 is an important DNA binding site. It has been shown to be the site for cross-linking. | |||
Tryptophan and Lysine residues are important in binding as well. Treatments resulting in | |||
modification of arginine, cysteine, or tyrosine residues had no effect on binding of SSB to | |||
DNA, whereas modification of either lysine residues (with acetic anhydride) or tryptophan | |||
residues (with N-bromosuccinimide) led to complete loss of binding activity <ref>PMID: 2087220</ref>. | |||
The two tryptophan residues involved in DNA binding are Trp40 and Trp54, which was | |||
determined by mutagenesis. One more binding site was determined by site-specific mutagenesis. | |||
When His55 is substituted with Leu it decreases binding affinity. All of these residues | |||
are found in a hydrophobic region, which is suitable for nucleotide base interactions. | |||
</StructureSection> | |||
==See Also== | ==See Also== | ||
