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| | <StructureSection load='5fdk' size='340' side='right'caption='[[5fdk]], [[Resolution|resolution]] 3.21Å' scene=''> | | <StructureSection load='5fdk' size='340' side='right'caption='[[5fdk]], [[Resolution|resolution]] 3.21Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fdk]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FDK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FDK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fdk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FDK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FDK FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zp7|1zp7]]</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]] 3.208Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">recU, prfA, yppB, BSU22310 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=5fdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fdk OCA], [https://pdbe.org/5fdk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fdk RCSB], [https://www.ebi.ac.uk/pdbsum/5fdk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fdk ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fdk OCA], [http://pdbe.org/5fdk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fdk RCSB], [http://www.ebi.ac.uk/pdbsum/5fdk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fdk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RECU_BACSU RECU_BACSU]] Has at least 2 separable functions; Holliday junction resolution with generation of monomeric chromosomes, and modulation of RecA activity. Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation. Partially inhibits the hydrolysis of dATP or rATP by RecA. Holliday junction resolution is stimulated by RuvB.<ref>PMID:14701911</ref> <ref>PMID:16020779</ref> <ref>PMID:16154091</ref> | + | [https://www.uniprot.org/uniprot/RECU_BACSU RECU_BACSU] Has at least 2 separable functions; Holliday junction resolution with generation of monomeric chromosomes, and modulation of RecA activity. Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation. Partially inhibits the hydrolysis of dATP or rATP by RecA. Holliday junction resolution is stimulated by RuvB.<ref>PMID:14701911</ref> <ref>PMID:16020779</ref> <ref>PMID:16154091</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kale, A]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Khavnekar, S]] | + | [[Category: Kale A]] |
| - | [[Category: Rafferty, J B]] | + | [[Category: Khavnekar S]] |
| - | [[Category: Complex]] | + | [[Category: Rafferty JB]] |
| - | [[Category: Dna]]
| + | |
| - | [[Category: Dna-binding protein]]
| + | |
| - | [[Category: Holliday junction]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Recu]]
| + | |
| - | [[Category: Resolvase]]
| + | |
| Structural highlights
Function
RECU_BACSU Has at least 2 separable functions; Holliday junction resolution with generation of monomeric chromosomes, and modulation of RecA activity. Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation. Partially inhibits the hydrolysis of dATP or rATP by RecA. Holliday junction resolution is stimulated by RuvB.[1] [2] [3]
Publication Abstract from PubMed
Holliday junction (HJ) resolving enzyme RecU is involved in DNA repair and recombination. We have determined the crystal structure of inactive mutant (D88N) of RecU from Bacillus subtilis in complex with a 12 base palindromic DNA fragment at a resolution of 3.2 A. This structure shows the stalk region and the essential N-terminal region (NTR) previously unseen in our DNA unbound structure. The flexible nature of the NTR in solution was confirmed using SAXS. Thermofluor studies performed to assess the stability of RecU in complex with the arms of an HJ indicate that it confers stability. Further, we performed molecular dynamics (MD) simulations of wild type and an NTR deletion variant of RecU, with and without HJ. The NTR is observed to be highly flexible in simulations of the unbound RecU, in agreement with SAXS observations. These simulations revealed domain dynamics of RecU and their role in the formation of complex with HJ. The MD simulations also elucidate key roles of the NTR, stalk region, and breathing motion of RecU in the formation of the reactive state.
Structural insights into dynamics of RecU-HJ complex formation elucidates key role of NTR and stalk region toward formation of reactive state.,Khavnekar S, Dantu SC, Sedelnikova S, Ayora S, Rafferty J, Kale A Nucleic Acids Res. 2016 Nov 29. pii: gkw1165. PMID:27903910[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ayora S, Carrasco B, Doncel-Perez E, Lurz R, Alonso JC. Bacillus subtilis RecU protein cleaves Holliday junctions and anneals single-stranded DNA. Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):452-7. Epub 2003 Dec 30. PMID:14701911 doi:http://dx.doi.org/10.1073/pnas.2533829100
- ↑ Sanchez H, Kidane D, Reed P, Curtis FA, Cozar MC, Graumann PL, Sharples GJ, Alonso JC. The RuvAB branch migration translocase and RecU Holliday junction resolvase are required for double-stranded DNA break repair in Bacillus subtilis. Genetics. 2005 Nov;171(3):873-83. Epub 2005 Jul 14. PMID:16020779 doi:http://dx.doi.org/genetics.105.045906
- ↑ McGregor N, Ayora S, Sedelnikova S, Carrasco B, Alonso JC, Thaw P, Rafferty J. The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence-specific cleavage. Structure. 2005 Sep;13(9):1341-51. PMID:16154091 doi:10.1016/j.str.2005.05.011
- ↑ Khavnekar S, Dantu SC, Sedelnikova S, Ayora S, Rafferty J, Kale A. Structural insights into dynamics of RecU-HJ complex formation elucidates key role of NTR and stalk region toward formation of reactive state. Nucleic Acids Res. 2016 Nov 29. pii: gkw1165. PMID:27903910 doi:http://dx.doi.org/10.1093/nar/gkw1165
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