1M55

Catalytic domain of the Adeno Associated Virus type 5 Rep protein

Summary for 1M55

• Entry DOI: 10.2210/pdb1m55/pdb
• Descriptor: Rep protein, ZINC ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: endonuclease, rep, rolling circle replication, adeno-associated virus, viral protein
• Biological source: Adeno-associated virus - 5
• Total number of polymer chains: 2
• Total formula weight: 46017.32

Authors

Hickman, A.B.,Ronning, D.R.,Kotin, R.M.,Dyda, F. (deposition date: 2002-07-08, release date: 2002-08-28, Last modification date: 2024-02-14)

Primary citation

Hickman, A.B.,Ronning, D.R.,Kotin, R.M.,Dyda, F.
Structural unity among viral origin binding proteins: crystal structure of the nuclease domain of adeno-associated virus Rep.
Mol.Cell, 10:327-337, 2002

PubMed Abstract: Adeno-associated virus (AAV), unique among animal viruses in its ability to integrate into a specific chromosomal location, is a promising vector for human gene therapy. AAV Replication (Rep) protein is essential for viral replication and integration, and its amino terminal domain possesses site-specific DNA binding and endonuclease activities required for replication initiation and integration. This domain displays a novel endonuclease fold and demonstrates an unexpected structural relationship to other viral origin binding proteins such as the papillomavirus E1 protein and the SV40 T antigen. The active site, located at the bottom of a positively charged cleft, is formed by the spatial convergence of a divalent metal ion and two conserved sequence motifs that define the rolling circle replication superfamily.

PubMed: 12191478
DOI: 10.1016/S1097-2765(02)00592-0

Experimental method

X-RAY DIFFRACTION (1.4 Å)