1rz9
From Proteopedia
(New page: 200px<br /><applet load="1rz9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rz9, resolution 3.10Å" /> '''Crystal Structure of...) |
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| - | [[Image:1rz9.gif|left|200px]]<br /><applet load="1rz9" size=" | + | [[Image:1rz9.gif|left|200px]]<br /><applet load="1rz9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rz9, resolution 3.10Å" /> | caption="1rz9, resolution 3.10Å" /> | ||
'''Crystal Structure of AAV Rep complexed with the Rep-binding sequence'''<br /> | '''Crystal Structure of AAV Rep complexed with the Rep-binding sequence'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Integration into a particular location in human chromosomes is a unique | + | 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== | ==About this Structure== | ||
| - | 1RZ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Adeno-associated_virus_-_5 Adeno-associated virus - 5]. Full crystallographic information is available from [http:// | + | 1RZ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Adeno-associated_virus_-_5 Adeno-associated virus - 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZ9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dyda, F.]] | [[Category: Dyda, F.]] | ||
| - | [[Category: Hickman, A | + | [[Category: Hickman, A B.]] |
| - | [[Category: Kotin, R | + | [[Category: Kotin, R M.]] |
| - | [[Category: Perez, Z | + | [[Category: Perez, Z N.]] |
| - | [[Category: Ronning, D | + | [[Category: Ronning, D R.]] |
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:18 2008'' |
Revision as of 12:56, 21 February 2008
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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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