1in7: Difference between revisions

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<StructureSection load='1in7' size='340' side='right'caption='[[1in7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1in7' size='340' side='right'caption='[[1in7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1in7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IN7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1in7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IN7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1in4|1in4]], [[1in5|1in5]], [[1in6|1in6]], [[1in8|1in8]], [[1j7k|1j7k]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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">RuvB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=1in7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1in7 OCA], [https://pdbe.org/1in7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1in7 RCSB], [https://www.ebi.ac.uk/pdbsum/1in7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1in7 ProSAT]</span></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=1in7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1in7 OCA], [https://pdbe.org/1in7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1in7 RCSB], [https://www.ebi.ac.uk/pdbsum/1in7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1in7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RUVB_THEMA RUVB_THEMA]] The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing (By similarity).  
[https://www.uniprot.org/uniprot/RUVB_THEMA RUVB_THEMA] The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43589]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Clancy, S B]]
[[Category: Thermotoga maritima]]
[[Category: Putnam, C D]]
[[Category: Clancy SB]]
[[Category: Tainer, J A]]
[[Category: Putnam CD]]
[[Category: Tsuruta, H]]
[[Category: Tainer JA]]
[[Category: Wetmur, J G]]
[[Category: Tsuruta H]]
[[Category: Aaa+-class atpase]]
[[Category: Wetmur JG]]
[[Category: Arginine finger]]
[[Category: Branch migration]]
[[Category: Dna binding protein]]
[[Category: Dna translocase]]
[[Category: Holliday junction]]
[[Category: Sensor 1]]
[[Category: Sensor 2]]
[[Category: Walker some]]
[[Category: Walker b]]
[[Category: Winged-helix domain]]

Latest revision as of 11:35, 16 August 2023

THERMOTOGA MARITIMA RUVB R170ATHERMOTOGA MARITIMA RUVB R170A

Structural highlights

1in7 is a 1 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RUVB_THEMA The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The RuvB hexamer is the chemomechanical motor of the RuvAB complex that migrates Holliday junction branch-points in DNA recombination and the rescue of stalled DNA replication forks. The 1.6 A crystal structure of Thermotoga maritima RuvB together with five mutant structures reveal that RuvB is an ATPase-associated with diverse cellular activities (AAA+-class ATPase) with a winged-helix DNA-binding domain. The RuvB-ADP complex structure and mutagenesis suggest how AAA+-class ATPases couple nucleotide binding and hydrolysis to interdomain conformational changes and asymmetry within the RuvB hexamer implied by the crystallographic packing and small-angle X-ray scattering in solution. ATP-driven domain motion is positioned to move double-stranded DNA through the hexamer and drive conformational changes between subunits by altering the complementary hydrophilic protein- protein interfaces. Structural and biochemical analysis of five motifs in the protein suggest that ATP binding is a strained conformation recognized both by sensors and the Walker motifs and that intersubunit activation occurs by an arginine finger motif reminiscent of the GTPase-activating proteins. Taken together, these results provide insights into how RuvB functions as a motor for branch migration of Holliday junctions.

Structure and mechanism of the RuvB Holliday junction branch migration motor.,Putnam CD, Clancy SB, Tsuruta H, Gonzalez S, Wetmur JG, Tainer JA J Mol Biol. 2001 Aug 10;311(2):297-310. PMID:11478862[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Putnam CD, Clancy SB, Tsuruta H, Gonzalez S, Wetmur JG, Tainer JA. Structure and mechanism of the RuvB Holliday junction branch migration motor. J Mol Biol. 2001 Aug 10;311(2):297-310. PMID:11478862 doi:http://dx.doi.org/10.1006/jmbi.2001.4852

1in7, resolution 1.90Å

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