5ja4

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'''Unreleased structure'''
 
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The entry 5ja4 is ON HOLD until Paper Publication
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==Crystal structure of human TONSL and MCM2 HBDs binding to a histone H3-H4 tetramer==
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<StructureSection load='5ja4' size='340' side='right' caption='[[5ja4]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ja4]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JA4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JA4 FirstGlance]. <br>
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Description:
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>
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<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=5ja4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ja4 OCA], [http://pdbe.org/5ja4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ja4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ja4 PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/TONSL_HUMAN TONSL_HUMAN]] Component of the MMS22L-TONSL complex, a complex that stimulates the recombination-dependent repair of stalled or collapsed replication forks. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication by promoting homologous recombination-mediated repair of replication fork-associated double-strand breaks. It may act by mediating the assembly of RAD51 filaments on ssDNA. Within the complex, may act as a scaffold.<ref>PMID:21055983</ref> <ref>PMID:21055984</ref> <ref>PMID:21055985</ref> <ref>PMID:7738005</ref> [[http://www.uniprot.org/uniprot/MCM2_HUMAN MCM2_HUMAN]] Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division.<ref>PMID:8175912</ref>
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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: DNA helicase]]
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[[Category: Huang, H]]
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[[Category: Patel, D]]
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[[Category: Chaperone]]
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[[Category: Dna repair and histone chaperone]]

Revision as of 22:27, 20 June 2016

Crystal structure of human TONSL and MCM2 HBDs binding to a histone H3-H4 tetramer

5ja4, resolution 2.42Å

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