1uut

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[[Image:1uut.gif|left|200px]]<br /><applet load="1uut" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1uut.gif|left|200px]]
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caption="1uut, resolution 2.0&Aring;" />
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'''THE NUCLEASE DOMAIN OF ADENO-ASSOCIATED VIRUS REP COMPLEXED WITH THE RBE' STEMLOOP OF THE VIRAL INVERTED TERMINAL REPEAT'''<br />
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{{Structure
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|PDB= 1uut |SIZE=350|CAPTION= <scene name='initialview01'>1uut</scene>, resolution 2.0&Aring;
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+C'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''THE NUCLEASE DOMAIN OF ADENO-ASSOCIATED VIRUS REP COMPLEXED WITH THE RBE' STEMLOOP OF THE VIRAL INVERTED TERMINAL REPEAT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UUT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Adeno-associated_virus_-_5 Adeno-associated virus - 5] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+C'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUT OCA].
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1UUT is a [[Protein complex]] structure of sequences 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=1UUT OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14967147 14967147]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14967147 14967147]
[[Category: Adeno-associated virus - 5]]
[[Category: Adeno-associated virus - 5]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: viral protein]]
[[Category: viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:37:04 2008''

Revision as of 12:37, 20 March 2008


PDB ID 1uut

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, resolution 2.0Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



THE NUCLEASE DOMAIN OF ADENO-ASSOCIATED VIRUS REP COMPLEXED WITH THE RBE' STEMLOOP OF THE VIRAL INVERTED TERMINAL REPEAT


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

1UUT is a Protein complex structure of sequences 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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