4d2i

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the HerA hexameric DNA translocase from Sulfolobus solfataricus bound to AMP-PNP

Structural highlights

4d2i is a 2 chain structure with sequence from Saccharolobus solfataricus P2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.841Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HERA_SACS2 Involved in DNA double-strand break (DSB) repair (PubMed:22135300). Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity (PubMed:22135300, PubMed:25420454).[UniProtKB:Q8U1P0]^[1] ^[2]

Publication Abstract from PubMed

The HerA ATPase cooperates with the NurA nuclease and the Mre11-Rad50 complex for the repair of double-strand DNA breaks in thermophilic archaea. Here we extend our structural knowledge of this minimal end-resection apparatus by presenting the first crystal structure of hexameric HerA. The full-length structure visualizes at atomic resolution the N-terminal HerA-ATP synthase domain and a conserved C-terminal extension, which acts as a physical brace between adjacent protomers. The brace also interacts in trans with nucleotide-binding residues of the neighbouring subunit. Our observations support a model in which the coaxial interaction of the HerA ring with the toroidal NurA dimer generates a continuous channel traversing the complex. HerA-driven translocation would propel the DNA towards the narrow annulus of NurA, leading to duplex melting and nucleolytic digestion. This system differs substantially from the bacterial end-resection paradigms. Our findings suggest a novel mode of DNA-end processing by this integrated archaeal helicase-nuclease machine.

Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea.,Rzechorzek NJ, Blackwood JK, Bray SM, Maman JD, Pellegrini L, Robinson NP Nat Commun. 2014 Nov 25;5:5506. doi: 10.1038/ncomms6506. PMID:25420454^[3]

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

References

↑ Blackwood JK, Rzechorzek NJ, Abrams AS, Maman JD, Pellegrini L, Robinson NP. Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex. Nucleic Acids Res. 2011 Dec 1. PMID:22135300 doi:10.1093/nar/gkr1157
↑ Rzechorzek NJ, Blackwood JK, Bray SM, Maman JD, Pellegrini L, Robinson NP. Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea. Nat Commun. 2014 Nov 25;5:5506. doi: 10.1038/ncomms6506. PMID:25420454 doi:http://dx.doi.org/10.1038/ncomms6506
↑ Rzechorzek NJ, Blackwood JK, Bray SM, Maman JD, Pellegrini L, Robinson NP. Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea. Nat Commun. 2014 Nov 25;5:5506. doi: 10.1038/ncomms6506. PMID:25420454 doi:http://dx.doi.org/10.1038/ncomms6506

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4d2i"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the HerA hexameric DNA translocase from Sulfolobus solfataricus bound to AMP-PNP==
-<StructureSection load='4d2i' size='340' side='right' caption='[[4d2i]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
+<StructureSection load='4d2i' size='340' side='right'caption='[[4d2i]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4d2i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D2I FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4d2i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D2I FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.841&#8491;</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=4d2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2i OCA], [http://pdbe.org/4d2i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d2i RCSB], [http://www.ebi.ac.uk/pdbsum/4d2i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2i ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4d2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2i OCA], [https://pdbe.org/4d2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d2i RCSB], [https://www.ebi.ac.uk/pdbsum/4d2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2i ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/HERA_SACS2 HERA_SACS2] Involved in DNA double-strand break (DSB) repair (PubMed:22135300). Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity (PubMed:22135300, PubMed:25420454).[UniProtKB:Q8U1P0]<ref>PMID:22135300</ref> <ref>PMID:25420454</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Blackwood, J K]]
+[[Category: Large Structures]]
-[[Category: Bray, S M]]
+[[Category: Saccharolobus solfataricus P2]]
-[[Category: Maman, J D]]
+[[Category: Blackwood JK]]
-[[Category: Pellegrini, L]]
+[[Category: Bray SM]]
-[[Category: Robinson, N P]]
+[[Category: Maman JD]]
-[[Category: Rzechorzek, N J]]
+[[Category: Pellegrini L]]
-[[Category: Dna]]
+[[Category: Robinson NP]]
-[[Category: Helicase]]
+[[Category: Rzechorzek NJ]]
-[[Category: Homologous recombination]]
-[[Category: Hydrolase]]
-[[Category: Mre11]]
-[[Category: Nura]]
-[[Category: Rad50]]
-[[Category: Translocase]]

4d2i

From Proteopedia

Current revision

Crystal structure of the HerA hexameric DNA translocase from Sulfolobus solfataricus bound to AMP-PNP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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