This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1je5
From Proteopedia
|
Crystal Structure of gp2.5, a Single-Stranded DNA Binding Protein Encoded by Bacteriophage T7
Overview
The gene 2.5 protein (gp2.5) of bacteriophage T7 is a single-stranded DNA (ssDNA) binding protein that has essential roles in DNA replication and recombination. In addition to binding DNA, gp2.5 physically interacts with T7 DNA polymerase and T7 primase-helicase during replication to coordinate events at the replication fork. We have determined a 1.9-A crystal structure of gp2.5 and show that it has a conserved OB-fold (oligosaccharide/oligonucleotide binding fold) that is well adapted for interactions with ssDNA. Superposition of the OB-folds of gp2.5 and other ssDNA binding proteins reveals a conserved patch of aromatic residues that stack against the bases of ssDNA in the other crystal structures, suggesting that gp2.5 binds to ssDNA in a similar manner. An acidic C-terminal extension of the gp2.5 protein, which is required for dimer formation and for interactions with the T7 DNA polymerase and the primase-helicase, appears to be flexible and may act as a switch that modulates the DNA binding affinity of gp2.5.
About this Structure
1JE5 is a Single protein structure of sequence from Bacteriophage t7 with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the gene 2.5 protein, a single-stranded DNA binding protein encoded by bacteriophage T7., Hollis T, Stattel JM, Walther DS, Richardson CC, Ellenberger T, Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9557-62. Epub 2001 Jul 31. PMID:11481454
Page seeded by OCA on Thu Feb 21 13:21:36 2008
