2C5R

The structure of phage phi29 replication organizer protein p16.7 in complex with double stranded DNA

Summary for 2C5R

• Entry DOI: 10.2210/pdb2c5r/pdb
• Related: 1ZAE 2BNK
• Descriptor: EARLY PROTEIN P16.7, 5'-D(*TP*CP*CP*AP*CP*CP*GP*GP)-3', 5'-D(*CP*CP*GP*GP*TP*GP*GP*AP)-3', ... (4 entities in total)
• Functional Keywords: dna-binding protein-dna complex, dna-binding protein, complex (dna-binding protein-dna), dna-binding protein/dna
• Biological source: BACILLUS PHAGE PHI29
• Total number of polymer chains: 8
• Total formula weight: 52483.03

Authors

Albert, A.,Jimenez, M.,Munoz-Espin, D.,Asensio, J.L.,Hermoso, J.A.,Salas, M.,Meijer, W.J.J. (deposition date: 2005-10-31, release date: 2005-11-08, Last modification date: 2023-12-13)

Primary citation

Albert, A.,Munoz-Espin, D.,Jimenez, M.,Asensio, J.L.,Hermoso, J.A.,Salas, M.,Meijer, W.J.J.
Structural Basis for Membrane Anchorage of Viral Phi 29 DNA During Replication.
J.Biol.Chem., 280:42486-, 2005

PubMed Abstract: Prokaryotic DNA replication is compartmentalized at the cellular membrane. Functional and biochemical studies showed that the Bacillus subtilis phage 29-encoded membrane protein p16.7 is directly involved in the organization of membrane-associated viral DNA replication. The structure of the functional domain of p16.7 in complex with DNA, presented here, reveals the multimerization mode of the protein and provides insights in the organization of the phage genome at the membrane of the infected cell.

PubMed: 16275651
DOI: 10.1074/JBC.C500429200

Experimental method

X-RAY DIFFRACTION (2.9 Å)