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| | <StructureSection load='4ww4' size='340' side='right'caption='[[4ww4]], [[Resolution|resolution]] 2.94Å' scene=''> | | <StructureSection load='4ww4' size='340' side='right'caption='[[4ww4]], [[Resolution|resolution]] 2.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ww4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WW4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ww4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WW4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0006820 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD]), CTHT_0006170 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</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=4ww4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ww4 OCA], [https://pdbe.org/4ww4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ww4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ww4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ww4 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ww4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ww4 OCA], [http://pdbe.org/4ww4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ww4 RCSB], [http://www.ebi.ac.uk/pdbsum/4ww4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ww4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0RYI5_CHATD G0RYI5_CHATD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4ww4" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4ww4" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Helicase 3D structures|Helicase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| - | [[Category: DNA helicase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hopfner, K P]] | + | [[Category: Hopfner K-P]] |
| - | [[Category: Lakomek, K]] | + | [[Category: Lakomek K]] |
| - | [[Category: Aaa+ atpase]]
| + | |
| - | [[Category: Adp-bound state]]
| + | |
| - | [[Category: Dodecameric assembly]]
| + | |
| - | [[Category: Full-length protein]]
| + | |
| - | [[Category: Hexameric ring]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
G0RYI5_CHATD
Publication Abstract from PubMed
As building blocks of diverse macromolecular complexes, the AAA+ ATPases Rvb1 and Rvb2 are crucial for many cellular activities including cancer-related processes. Their oligomeric structure and function remain unclear. We report the crystal structures of full-length heteromeric Rvb1.Rvb2 complexes in distinct nucleotide binding states. Chaetomium thermophilum Rvb1.Rvb2 assemble into hexameric rings of alternating molecules and into stable dodecamers. Intriguingly, the characteristic oligonucleotide-binding (OB) fold domains (DIIs) of Rvb1 and Rvb2 occupy unequal places relative to the compact AAA+ core ring. While Rvb1's DII forms contacts between hexamers, Rvb2's DII is rotated 100 degrees outward, occupying lateral positions. ATP was retained bound to Rvb1 but not Rvb2 throughout purification, suggesting nonconcerted ATPase activities and nucleotide binding. Significant conformational differences between nucleotide-free and ATP-/ADP-bound states in the crystal structures and in solution suggest that the functional role of Rvb1.Rvb2 is mediated by highly interconnected structural switches. Our structures provide an atomic framework for dodecameric states and Rvb1.Rvb2's conformational plasticity.
Structural Basis for Dodecameric Assembly States and Conformational Plasticity of the Full-Length AAA+ ATPases Rvb1.Rvb2.,Lakomek K, Stoehr G, Tosi A, Schmailzl M, Hopfner KP Structure. 2015 Feb 5. pii: S0969-2126(14)00424-9. doi:, 10.1016/j.str.2014.12.015. PMID:25661652[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lakomek K, Stoehr G, Tosi A, Schmailzl M, Hopfner KP. Structural Basis for Dodecameric Assembly States and Conformational Plasticity of the Full-Length AAA+ ATPases Rvb1.Rvb2. Structure. 2015 Feb 5. pii: S0969-2126(14)00424-9. doi:, 10.1016/j.str.2014.12.015. PMID:25661652 doi:http://dx.doi.org/10.1016/j.str.2014.12.015
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