6zff
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6zff is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures) |
|||
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Pyrococcus furiosus Rad50 coiled coils in rod configuration== | |
| + | <StructureSection load='6zff' size='340' side='right'caption='[[6zff]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6zff]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZFF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZFF FirstGlance]. <br> | ||
| + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rad50, PF1167 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</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=6zff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zff OCA], [http://pdbe.org/6zff PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zff RCSB], [http://www.ebi.ac.uk/pdbsum/6zff PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zff ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_PYRFU]] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Rad50-Mre11 nuclease complex plays a vital role in DNA repair in all domains of life. It recognizes and processes DNA double-strand breaks. Rad50 proteins fold into an extended structure with a ~ 20-60 nm long coiled coil connecting a globular ABC ATPase domain with a zinc hook dimerization domain. A published structure of an archaeal Rad50 zinc hook shows coiled coils pointing away from each other. Here we present the crystal structure of an alternate conformation displaying co-aligned coiled coils. Archaeal Rad50 may thus switch between rod-shaped and ring-like conformations as recently proposed for a bacterial homolog. This article is protected by copyright. All rights reserved. | ||
| - | + | A rod conformation of the Pyrococcus furiosus Rad50 coiled coil.,Soh YM, Basquin J, Gruber S Proteins. 2020 Sep 2. doi: 10.1002/prot.26005. PMID:32875643<ref>PMID:32875643</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6zff" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyrfu]] | ||
| + | [[Category: Basquin, J]] | ||
| + | [[Category: Gruber, S]] | ||
| + | [[Category: Soh, Y M]] | ||
| + | [[Category: Closed coiled coil arm]] | ||
| + | [[Category: Dna]] | ||
| + | [[Category: Dna damge response]] | ||
| + | [[Category: Double strand break repair]] | ||
| + | [[Category: Scaffold]] | ||
Current revision
Pyrococcus furiosus Rad50 coiled coils in rod configuration
| |||||||||||
