6s85
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cutting state of the E. coli Mre11-Rad50 (SbcCD) head complex bound to ADP and dsDNA.== | |
| + | <StructureSection load='6s85' size='340' side='right'caption='[[6s85]], [[Resolution|resolution]] 4.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6s85]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S85 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sbcC, A9R57_08510, ACU57_12010, AM464_18965, AUQ13_18525, BANRA_02011, BANRA_03598, BHS87_02160, BJJ90_20275, BUE81_15555, BW690_06605, C4J69_09480, C5N07_12770, C9E25_04550, CA593_01155, D0X26_07450, D3821_12870, D3Y67_14380, D9D20_11475, D9F57_05650, DNQ41_05895, EAI52_02975, EC3426_01234, EL75_3354, EL79_3449, EL80_3403, ERS085365_01836, ERS085416_01964, ERS139211_01256, ERS150873_01854, NCTC13462_01932, NCTC9037_03952, RK56_026675, SAMEA3446340_01460, SAMEA3472047_02107, SAMEA3484427_03539, SAMEA3484429_01893, SAMEA3752559_02893, SAMEA3753300_00462, SK85_00422 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), sbcD, A9R57_08515, ACU90_20930, AM270_02320, AM464_18970, AMK83_08850, AML07_05375, APZ14_19360, ARC77_21640, AU473_24540, AUQ13_18520, AUS26_08295, AW106_10255, AWF80_027335, B1K96_09895, BANRA_00933, BANRA_02010, BANRA_03599, BB545_15570, BHS81_02440, BHS87_02165, BJJ90_20270, BK292_14605, BMT53_08385, BMT91_05280, BN17_02021, BTQ04_02895, BTQ06_17755, BUE81_15560, BVL39_00845, BW690_06610, BWP17_02185, C2U48_08075, C4J69_09475, C5N07_12775, C5P01_16270, C5P43_02310, C6986_02395, C7235_18845, C7B08_06215, C9E25_04545, CA593_01150, CG691_03340, CG705_03245, CG706_02645, COD30_16020, COD46_04825, CR538_19460, CRE06_07850, CVH05_20670, CWS33_22910, D0X26_07455, D2184_11480, D3821_12865, D3822_22430, D3O91_15270, D3Y67_14385, D4M06_05505, D7K63_09095, D7K66_05465, D9H94_07055, D9I87_03345, D9I97_02300, D9J44_05860, D9L89_06325, D9X97_05375, DIV22_26320, DL455_04405, DL545_19095, DL800_03920, DMI04_05300, DMZ31_02500, DNB37_05400, DNQ41_05900, DOY56_05885, DQF57_07710, DQO13_05535, DS732_06955, DTL43_07380, E2855_00535, E2863_00431, EAI44_12705, EAI52_02980, EB509_06820, EB510_01660, EB515_09310, EC1094V2_3455, EC3234A_4c00670, EC3426_01235, EC95NR1_04617, ECs0448, ED225_07565, ED287_10145, ED600_06285, ED607_18305, ED611_06615, ED903_13690, ED944_09545, EEA45_02820, EEP23_01080, EF173_10600, EFV01_15655, EFV11_06690, EFV17_08300, EIA13_09680, EL75_3353, EL79_3448, EL80_3402, ERS085365_01835, ERS085379_01210, ERS085416_01963, ERS139211_01257, ERS150873_01853, ERS150876_00572, FORC28_4694, HW43_05600, NCTC10090_01877, NCTC10429_03756, NCTC11022_05144, NCTC13125_01885, NCTC13127_05149, NCTC13462_01931, NCTC8009_07006, NCTC8179_01650, NCTC8960_01309, NCTC9036_03833, NCTC9037_03951, NCTC9045_04425, NCTC9055_00697, NCTC9058_03126, NCTC9062_04472, NCTC9111_03972, NCTC9703_03216, NCTC9706_01107, PU06_02925, RG28_02875, RK56_026670, RX35_02069, SAMEA3446340_01461, SAMEA3472043_02687, SAMEA3472044_00460, SAMEA3472047_02108, SAMEA3472055_02158, SAMEA3472070_02276, SAMEA3472114_01252, SAMEA3484427_03538, SAMEA3484429_01894, SAMEA3752553_00281, SAMEA3752559_02892, SAMEA3753064_01241, SAMEA3753097_00507, SAMEA3753290_01730, SAMEA3753300_00463, SK85_00423, WR15_04330 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=6s85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s85 OCA], [http://pdbe.org/6s85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s85 RCSB], [http://www.ebi.ac.uk/pdbsum/6s85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s85 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A037YDI0_ECOLX A0A037YDI0_ECOLX]] SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity.[RuleBase:RU363070] [[http://www.uniprot.org/uniprot/C3TMC7_ECOLX C3TMC7_ECOLX]] SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity.[RuleBase:RU363069] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | DNA double-strand breaks (DSBs) threaten genome stability throughout life and are linked to tumorigenesis in humans. To initiate DSB repair by end joining or homologous recombination, the Mre11-nuclease Rad50-ATPase complex detects and processes diverse and obstructed DNA ends, but a structural mechanism is still lacking. Here we report cryo-EM structures of the E. coli Mre11-Rad50 homolog SbcCD in resting and DNA-bound cutting states. In the resting state, Mre11's nuclease is blocked by ATP-Rad50, and the Rad50 coiled coils appear flexible. Upon DNA binding, the two coiled coils zip up into a rod and, together with the Rad50 nucleotide-binding domains, form a clamp around dsDNA. Mre11 moves to the side of Rad50, binds the DNA end, and assembles a DNA cutting channel for the nuclease reactions. The structures reveal how Mre11-Rad50 can detect and process diverse DNA ends and uncover a clamping and gating function for the coiled coils. | ||
| - | + | Mechanism of DNA End Sensing and Processing by the Mre11-Rad50 Complex.,Kashammer L, Saathoff JH, Lammens K, Gut F, Bartho J, Alt A, Kessler B, Hopfner KP Mol Cell. 2019 Nov 7;76(3):382-394.e6. doi: 10.1016/j.molcel.2019.07.035. Epub, 2019 Sep 3. PMID:31492634<ref>PMID:31492634</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6s85" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus coli migula 1895]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Alt, A]] | ||
| + | [[Category: Bartho, J]] | ||
| + | [[Category: Gut, F]] | ||
| + | [[Category: Hopfner, K P]] | ||
| + | [[Category: Kaeshammer, L]] | ||
| + | [[Category: Kessler, B]] | ||
| + | [[Category: Lammens, K]] | ||
| + | [[Category: Saathoff, J H]] | ||
| + | [[Category: Abc-type atpase]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Dna double-strand break]] | ||
| + | [[Category: Dna repair]] | ||
| + | [[Category: Nuclease]] | ||
Revision as of 17:58, 20 November 2019
Cutting state of the E. coli Mre11-Rad50 (SbcCD) head complex bound to ADP and dsDNA.
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