4tmu
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of RecQ catalytic core from C. sakazakii bound to DNA== | |
| + | <StructureSection load='4tmu' size='340' side='right'caption='[[4tmu]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4tmu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cronobacter_sakazakii_ATCC_BAA-894 Cronobacter sakazakii ATCC BAA-894] 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=4TMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TMU FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4tmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tmu OCA], [https://pdbe.org/4tmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tmu RCSB], [https://www.ebi.ac.uk/pdbsum/4tmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tmu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A7MQK9_CROS8 A7MQK9_CROS8] | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4tmu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cronobacter sakazakii ATCC BAA-894]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Keck JL]] | ||
| + | [[Category: Manthei KA]] | ||
Current revision
Crystal structure of RecQ catalytic core from C. sakazakii bound to DNA
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