4tmu: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 4tmu is ON HOLD  until Paper Publication
==Crystal structure of RecQ catalytic core from C. sakazakii bound to DNA==
<StructureSection load='4tmu' size='340' side='right'caption='[[4tmu]], [[Resolution|resolution]] 2.40&Aring;' 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]] 2.4&#8491;</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.


Authors: Manthei, K.A., Keck, J.L.
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Keck, J.L]]
<div class="pdbe-citations 4tmu" style="background-color:#fffaf0;"></div>
[[Category: Manthei, K.A]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cronobacter sakazakii ATCC BAA-894]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Keck JL]]
[[Category: Manthei KA]]
Retrieved from "https://proteopedia.org/4tmu"