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| | <StructureSection load='4yke' size='340' side='right'caption='[[4yke]], [[Resolution|resolution]] 2.78Å' scene=''> | | <StructureSection load='4yke' size='340' side='right'caption='[[4yke]], [[Resolution|resolution]] 2.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yke]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YKE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YKE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4yke]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YKE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.783Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0007600 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=4yke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yke OCA], [http://pdbe.org/4yke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yke RCSB], [http://www.ebi.ac.uk/pdbsum/4yke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yke ProSAT]</span></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=4yke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yke OCA], [https://pdbe.org/4yke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yke RCSB], [https://www.ebi.ac.uk/pdbsum/4yke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yke ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0RYR3_CHATD G0RYR3_CHATD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hopfner, K P]] | + | [[Category: Hopfner K-P]] |
| - | [[Category: Lammens, K]] | + | [[Category: Lammens K]] |
| - | [[Category: Seifert, F U]] | + | [[Category: Seifert FU]] |
| - | [[Category: Catalytic domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Nuclease]]
| + | |
| - | [[Category: Protein binding]]
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| Structural highlights
Function
G0RYR3_CHATD
Publication Abstract from PubMed
Together with the Rad50 ATPase, the Mre11 nuclease forms an evolutionarily conserved protein complex that plays a central role in the repair of DNA double-strand breaks (DSBs). Mre11-Rad50 detects and processes DNA ends, and has functions in the tethering as well as the signalling of DSBs. The Mre11 dimer can bind one or two DNA ends or hairpins, and processes DNA endonucleolytically as well as exonucleolytically in the 3'-to-5' direction. Here, the crystal structure of the Mre11 catalytic domain dimer from Chaetomium thermophilum (CtMre11(CD)) is reported. CtMre11(CD) crystals diffracted to 2.8 A resolution and revealed previously undefined features within the dimer interface, in particular fully ordered eukaryote-specific insertion loops that considerably expand the dimer interface. Furthermore, comparison with other eukaryotic Mre11 structures reveals differences in the conformations of the dimer and the capping domain. In summary, the results reported here provide new insights into the architecture of the eukaryotic Mre11 dimer.
Structure of the catalytic domain of Mre11 from Chaetomium thermophilum.,Seifert FU, Lammens K, Hopfner KP Acta Crystallogr F Struct Biol Commun. 2015 Jun 1;71(Pt 6):752-7. doi:, 10.1107/S2053230X15007566. Epub 2015 May 22. PMID:26057807[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Seifert FU, Lammens K, Hopfner KP. Structure of the catalytic domain of Mre11 from Chaetomium thermophilum. Acta Crystallogr F Struct Biol Commun. 2015 Jun 1;71(Pt 6):752-7. doi:, 10.1107/S2053230X15007566. Epub 2015 May 22. PMID:26057807 doi:http://dx.doi.org/10.1107/S2053230X15007566
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