1s9h
From Proteopedia
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==Crystal Structure of Adeno-associated virus Type 2 Rep40== | ==Crystal Structure of Adeno-associated virus Type 2 Rep40== | ||
| - | <StructureSection load='1s9h' size='340' side='right' caption='[[1s9h]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='1s9h' size='340' side='right'caption='[[1s9h]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1s9h]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1s9h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Adeno-associated_virus_2 Adeno-associated virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S9H FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s9h OCA], [https://pdbe.org/1s9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s9h RCSB], [https://www.ebi.ac.uk/pdbsum/1s9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s9h ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/REP68_AAV2S REP68_AAV2S] Plays an essential role in the initiation of viral DNA synthesis. Binds specifically to an inverted terminal repeat element (ITR) on the 3' and 5' ends of the viral DNA, where it cleaves a site specifically to generate a priming site for initiation of the synthesis of a complementary strand. Plays also a role as transcriptional regulator, DNA helicase and as key factor in site-specific integration of the viral genome. Inhibits the host cell cycle G1/S and G2/M transitions. These arrests may provide essential cellular factors for viral DNA replication.<ref>PMID:9882364</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s9/1s9h_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s9/1s9h_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=1s9h ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | We report here the crystal structure of an SF3 DNA helicase, Rep40, from adeno-associated virus 2 (AAV2). We show that AAV2 Rep40 is structurally more similar to the AAA(+) class of cellular proteins than to DNA helicases from other superfamilies. The structure delineates the expected Walker A and B motifs, but also reveals an unexpected "arginine finger" that directly implies the requirement of Rep40 oligomerization for ATP hydrolysis and helicase activity. Further, the Rep40 AAA(+) domain is novel in that it is unimodular as opposed to bimodular. Altogether, the structural connection to AAA(+) proteins defines the general architecture of SF3 DNA helicases, a family that includes simian virus 40 (SV40) T antigen, as well as provides a conceptual framework for understanding the role of Rep proteins during AAV DNA replication, packaging, and site-specific integration. | ||
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| - | Crystal structure of the SF3 helicase from adeno-associated virus type 2.,James JA, Escalante CR, Yoon-Robarts M, Edwards TA, Linden RM, Aggarwal AK Structure. 2003 Aug;11(8):1025-35. PMID:12906833<ref>PMID:12906833</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Adeno-associated virus | + | [[Category: Adeno-associated virus 2]] |
| - | [[Category: Aggarwal | + | [[Category: Large Structures]] |
| - | [[Category: Edwards | + | [[Category: Aggarwal AK]] |
| - | [[Category: Escalante | + | [[Category: Edwards TA]] |
| - | [[Category: James | + | [[Category: Escalante CR]] |
| - | [[Category: Linden | + | [[Category: James JA]] |
| - | [[Category: Yoon-Robarts | + | [[Category: Linden RM]] |
| - | + | [[Category: Yoon-Robarts M]] | |
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Current revision
Crystal Structure of Adeno-associated virus Type 2 Rep40
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