4tmu
From Proteopedia
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<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=4tmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tmu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tmu RCSB], [http://www.ebi.ac.uk/pdbsum/4tmu PDBsum]</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=4tmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tmu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tmu RCSB], [http://www.ebi.ac.uk/pdbsum/4tmu PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | RecQ helicases unwind remarkably diverse DNA structures as key components of many cellular processes. How RecQ enzymes accommodate different substrates in a unified mechanism that couples ATP hydrolysis to DNA unwinding is unknown. Here, the X-ray crystal structure of the Cronobacter sakazakii RecQ catalytic core domain bound to duplex DNA with a 3' single-stranded extension identifies two DNA-dependent conformational rearrangements: a winged-helix domain pivots approximately 90 degrees to close onto duplex DNA, and a conserved aromatic-rich loop is remodeled to bind ssDNA. These changes coincide with a restructuring of the RecQ ATPase active site that positions catalytic residues for ATP hydrolysis. Complex formation also induces a tight bend in the DNA and melts a portion of the duplex. This bending, coupled with translocation, could provide RecQ with a mechanism for unwinding duplex and other DNA structures. | ||
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+ | Structural mechanisms of DNA binding and unwinding in bacterial RecQ helicases.,Manthei KA, Hill MC, Burke JE, Butcher SE, Keck JL Proc Natl Acad Sci U S A. 2015 Apr 7;112(14):4292-7. doi:, 10.1073/pnas.1416746112. Epub 2015 Mar 23. PMID:25831501<ref>PMID:25831501</ref> | ||
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+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 06:59, 15 April 2015
Crystal structure of RecQ catalytic core from C. sakazakii bound to DNA
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