3nbi

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(New page: '''Unreleased structure''' The entry 3nbi is ON HOLD Authors: Wang, F., Yang, Y., Singh, T.R., Busygina, V., Guo, R., Wan, K., Wang, W., Sung, P., Meetei, A.R., Lei, M. Description: Cr...)
Current revision (08:04, 9 October 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3nbi is ON HOLD
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==Crystal structure of human RMI1 N-terminus==
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<StructureSection load='3nbi' size='340' side='right'caption='[[3nbi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3nbi]] is a 1 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=3NBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NBI FirstGlance]. <br>
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbi OCA], [https://pdbe.org/3nbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nbi RCSB], [https://www.ebi.ac.uk/pdbsum/3nbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nbi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RMI1_HUMAN RMI1_HUMAN] Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability.<ref>PMID:15775963</ref> <ref>PMID:16595695</ref> <ref>PMID:16537486</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nb/3nbi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3nbi ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mutations in BLM, a RecQ-like helicase, are linked to the autosomal recessive cancer-prone disorder Bloom's syndrome. BLM associates with topoisomerase (Topo) IIIalpha, RMI1, and RMI2 to form the BLM complex that is essential for genome stability. The RMI1-RMI2 heterodimer stimulates the dissolution of double Holliday junction into non-crossover recombinants mediated by BLM-Topo IIIalpha and is essential for stabilizing the BLM complex. However, the molecular basis of these functions of RMI1 and RMI2 remains unclear. Here we report the crystal structures of multiple domains of RMI1-RMI2, providing direct confirmation of the existence of three oligonucleotide/oligosaccharide binding (OB)-folds in RMI1-RMI2. Our structural and biochemical analyses revealed an unexpected insertion motif in RMI1N-OB, which is important for stimulating the dHJ dissolution. We also revealed the structural basis of the interaction between RMI1C-OB and RMI2-OB and demonstrated the functional importance of the RMI1-RMI2 interaction in genome stability maintenance.
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Authors: Wang, F., Yang, Y., Singh, T.R., Busygina, V., Guo, R., Wan, K., Wang, W., Sung, P., Meetei, A.R., Lei, M.
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Crystal structures of RMI1 and RMI2, two OB-fold regulatory subunits of the BLM complex.,Wang F, Yang Y, Singh TR, Busygina V, Guo R, Wan K, Wang W, Sung P, Meetei AR, Lei M Structure. 2010 Sep 8;18(9):1159-70. PMID:20826342<ref>PMID:20826342</ref>
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Description: Crystal structure of human RMI1 N-terminus
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 10 10:59:36 2010''
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<div class="pdbe-citations 3nbi" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Busygina V]]
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[[Category: Guo R]]
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[[Category: Lei M]]
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[[Category: Meetei AR]]
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[[Category: Singh TR]]
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[[Category: Sung P]]
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[[Category: Wan K]]
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[[Category: Wang F]]
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[[Category: Wang W]]
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[[Category: Yang Y]]

Current revision

Crystal structure of human RMI1 N-terminus

PDB ID 3nbi

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