8GME
Crystal structure of the gp32-Dda-dT17 complex
Summary for 8GME
| Entry DOI | 10.2210/pdb8gme/pdb |
| Related | 8S9I |
| Descriptor | gp32, Dda helicase, dT17, ... (4 entities in total) |
| Functional Keywords | t4, gp32, dda, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Tequatrovirus T4 More |
| Total number of polymer chains | 6 |
| Total formula weight | 181715.34 |
| Authors | He, X.,Yun, M.K.,White, S.W. (deposition date: 2023-03-24, release date: 2023-06-28, Last modification date: 2025-01-22) |
| Primary citation | He, X.,Yun, M.K.,Li, Z.,Waddell, M.B.,Nourse, A.,Churion, K.A.,Kreuzer, K.N.,Byrd, A.K.,White, S.W. Structural and functional insights into the interaction between the bacteriophage T4 DNA processing proteins gp32 and Dda. Nucleic Acids Res., 52:12748-12762, 2024 Cited by PubMed Abstract: Bacteriophage T4 is a classic model system for studying the mechanisms of DNA processing. A key protein in T4 DNA processing is the gp32 single-stranded DNA-binding protein. gp32 has two key functions: it binds cooperatively to single-stranded DNA (ssDNA) to protect it from nucleases and remove regions of secondary structure, and it recruits proteins to initiate DNA processes including replication and repair. Dda is a T4 helicase recruited by gp32, and we purified and crystallized a gp32-Dda-ssDNA complex. The low-resolution structure revealed how the C-terminus of gp32 engages Dda. Analytical ultracentrifugation analyses were consistent with the crystal structure. An optimal Dda binding peptide from the gp32 C-terminus was identified using surface plasmon resonance. The crystal structure of the Dda-peptide complex was consistent with the corresponding interaction in the gp32-Dda-ssDNA structure. A Dda-dependent DNA unwinding assay supported the structural conclusions and confirmed that the bound gp32 sequesters the ssDNA generated by Dda. The structure of the gp32-Dda-ssDNA complex, together with the known structure of the gp32 body, reveals the entire ssDNA binding surface of gp32. gp32-Dda-ssDNA complexes in the crystal are connected by the N-terminal region of one gp32 binding to an adjacent gp32, and this provides key insights into this interaction. PubMed: 39417586DOI: 10.1093/nar/gkae910 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.98 Å) |
Structure validation
Download full validation report
