1rz9
From Proteopedia
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| - | [[Image:1rz9.gif|left|200px]] | ||
| - | + | ==Crystal Structure of AAV Rep complexed with the Rep-binding sequence== | |
| - | + | <StructureSection load='1rz9' size='340' side='right'caption='[[1rz9]], [[Resolution|resolution]] 3.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1rz9]] is a 7 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RZ9 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rz9 OCA], [https://pdbe.org/1rz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rz9 RCSB], [https://www.ebi.ac.uk/pdbsum/1rz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rz9 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | | | + | == Function == |
| - | + | [https://www.uniprot.org/uniprot/Q9YJC1_9VIRU Q9YJC1_9VIRU] | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rz/1rz9_consurf.spt"</scriptWhenChecked> | |
| - | == | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rz9 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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<ref>PMID:14967147</ref> | |
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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 | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 1rz9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Adeno-associated virus 5]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dyda F]] | ||
| + | [[Category: Hickman AB]] | ||
| + | [[Category: Kotin RM]] | ||
| + | [[Category: Perez ZN]] | ||
| + | [[Category: Ronning DR]] | ||
Current revision
Crystal Structure of AAV Rep complexed with the Rep-binding sequence
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