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5bnx
From Proteopedia
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| - | ''' | + | ==Crystal structure of Human MCM2 HBD and ASF1b chaperoning a histone H3.3-H4 dimer== |
| - | + | <StructureSection load='5bnx' size='340' side='right' caption='[[5bnx]], [[Resolution|resolution]] 2.31Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5bnx]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BNX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BNX FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bnv|5bnv]], [[5bo0|5bo0]]</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=5bnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bnx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bnx RCSB], [http://www.ebi.ac.uk/pdbsum/5bnx PDBsum]</span></td></tr> | |
| - | [[ | + | </table> |
| - | [[ | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/ASF1B_HUMAN ASF1B_HUMAN]] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly. Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA. Required for spermatogenesis.<ref>PMID:11897662</ref> <ref>PMID:12842904</ref> <ref>PMID:14718166</ref> <ref>PMID:15664198</ref> <ref>PMID:16151251</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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Huang, H]] | [[Category: Huang, H]] | ||
| + | [[Category: Patel, D J]] | ||
| + | [[Category: Asf1]] | ||
| + | [[Category: Chaperone-dna binding protein complex]] | ||
| + | [[Category: Dna replication]] | ||
| + | [[Category: H3 3-h4 dimer]] | ||
| + | [[Category: Mcm2]] | ||
Revision as of 15:34, 17 June 2015
Crystal structure of Human MCM2 HBD and ASF1b chaperoning a histone H3.3-H4 dimer
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