4hyy
From Proteopedia
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| - | {{STRUCTURE_4hyy| PDB=4hyy | SCENE= }} | ||
| - | ===Filament of octameric rings of DMC1 recombinase from Homo sapiens=== | ||
| - | {{ABSTRACT_PUBMED_23545642}} | ||
| - | == | + | ==Filament of octameric rings of DMC1 recombinase from Homo sapiens== |
| - | [[http://www.uniprot.org/uniprot/DMC1_HUMAN DMC1_HUMAN | + | <StructureSection load='4hyy' size='340' side='right'caption='[[4hyy]], [[Resolution|resolution]] 2.60Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4hyy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HYY 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]] 2.603Å</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=4hyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyy OCA], [https://pdbe.org/4hyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hyy RCSB], [https://www.ebi.ac.uk/pdbsum/4hyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hyy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DMC1_HUMAN DMC1_HUMAN] May participate in meiotic recombination, specifically in homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Eukaryal DMC1 proteins play a central role in homologous recombination in meiosis by assembling at the sites of programmed DNA double-strand breaks and carrying out a search for allelic DNA sequences located on homologous chromatids. They are close homologs of eukaryal Rad51 and archaeal RadA proteins and are remote homologs of bacterial RecA proteins. These recombinases (also called DNA strand-exchange proteins) promote a pivotal strand-exchange reaction between homologous single-stranded and double-stranded DNA substrates. An octameric form of a truncated human DMC1 devoid of its small N-terminal domain (residues 1-83) has been crystallized. The structure of the truncated DMC1 octamer is similar to that of the previously reported full-length DMC1 octamer, which has disordered N-terminal domains. In each protomer, only the ATP cap regions (Asp317-Glu323) show a noticeable conformational difference. The truncated DMC1 octamers further stack with alternate polarity into a filament. Similar filamentous assemblies of DMC1 have been observed to form on DNA by electron microscopy. | ||
| - | + | Structure of a filament of stacked octamers of human DMC1 recombinase.,Du L, Luo Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):382-6. doi:, 10.1107/S1744309113005678. Epub 2013 Mar 28. PMID:23545642<ref>PMID:23545642</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4hyy" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Du L]] |
| - | [[Category: | + | [[Category: Luo Y]] |
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Current revision
Filament of octameric rings of DMC1 recombinase from Homo sapiens
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