1rz9

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1rz9, resolution 3.10Å

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Crystal Structure of AAV Rep complexed with the Rep-binding sequence

Overview

Integration into a particular location in human chromosomes is a unique, property of the adeno-associated virus (AAV). This reaction requires the, viral Rep protein and AAV origin sequences. To understand how Rep, recognizes DNA, we have determined the structures of the Rep endonuclease, domain separately complexed with two DNA substrates: the Rep binding site, within the viral inverted terminal repeat and one of the terminal hairpin, arms. At the Rep binding site, five Rep monomers bind five tetranucleotide, direct repeats; each repeat is recognized by two Rep monomers from, opposing faces of the DNA. Stem-loop binding involves a protein interface, on the opposite side of the molecule from the active site where ssDNA is, cleaved. Rep therefore has three distinct binding sites within its, endonuclease domain for its different DNA substrates. Use of these, different interfaces generates the structural asymmetry necessary to, regulate later events in viral replication and integration.

About this Structure

1RZ9 is a Single protein structure of sequence from Adeno-associated virus - 5. Full crystallographic information is available from OCA.

Reference

The nuclease domain of adeno-associated virus rep coordinates replication initiation using two distinct DNA recognition interfaces., Hickman AB, Ronning DR, Perez ZN, Kotin RM, Dyda F, Mol Cell. 2004 Feb 13;13(3):403-14. PMID:14967147

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