Single stranded binding protein

From Proteopedia

Revision as of 22:35, 30 October 2013 by Rachel Craig (Talk | contribs)
Jump to: navigation, search

Contents

Sandbox Single Stranded DNA-Binding Protein (SSB)

Structure of Single Stranded DNA-Binding Protein bound to ssDNA (PDB entry 1eyg)

Drag the structure with the mouse to rotate

Binding Interactions in the Active Site

Phe-60 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” ( Meyer, 348). The two tryptophan residues involved in DNA binding are Try-40 and Try-54, which was determined by mutagenesis. One more binding site was determined by site-specific mutagenesis.

When His-55 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.

SSB-Protein Interactions

It is believed that Gly-15 may play an important role in binding the RecA protein. Mutations in Gly-15 have extreme effects on recombinational repair. SSB has also been thought to bind with exonuclease I, DNA polymerase II, and a protein n, which is used to help synthesize RNA primers for the lagging strand.

Structure of Single Stranded DNA-Binding Protein bound to ssDNA (PDB entry 1kaw)

Drag the structure with the mouse to rotate

See Also

References


PMID: 2087220

Proteopedia Page Contributors and Editors (what is this?)

Refayat Ahsen, Rachel Craig, Michal Harel, Alexander Berchansky

Personal tools