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| | ==The solution structure of CBD of human MCM6== | | ==The solution structure of CBD of human MCM6== |
| - | <StructureSection load='2klq' size='340' side='right' caption='[[2klq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2klq' size='340' side='right'caption='[[2klq]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2klq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KLQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KLQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2klq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KLQ FirstGlance]. <br> |
| - | </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=2klq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klq OCA], [http://pdbe.org/2klq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2klq RCSB], [http://www.ebi.ac.uk/pdbsum/2klq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2klq ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2klq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klq OCA], [https://pdbe.org/2klq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2klq RCSB], [https://www.ebi.ac.uk/pdbsum/2klq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2klq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MCM6_HUMAN MCM6_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.<ref>PMID:9305914</ref> | + | [https://www.uniprot.org/uniprot/MCM6_HUMAN MCM6_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.<ref>PMID:9305914</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Liu, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Atp-binding]] | + | [[Category: Liu C]] |
| - | [[Category: Cbd structure]]
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| - | [[Category: Cdt1]]
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| - | [[Category: Cell cycle]]
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| - | [[Category: Dna replication]]
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| - | [[Category: Dna-binding]]
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| - | [[Category: Mcm6]]
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| - | [[Category: Nucleotide-binding]]
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| - | [[Category: Nucleus]]
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| - | [[Category: Phosphoprotein]]
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| - | [[Category: Polymorphism]]
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| - | [[Category: Pre-rc]]
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| - | [[Category: Replication]]
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| - | [[Category: Transcription]]
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| - | [[Category: Transcription regulation]]
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| Structural highlights
Function
MCM6_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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The minichromosome maintenance (Mcm) 2-7 complex is the replicative helicase in eukaryotic species, and it plays essential roles in the initiation and elongation phases of DNA replication. During late M and early G(1), the Mcm2-7 complex is loaded onto chromatin to form prereplicative complex in a Cdt1-dependent manner. However, the detailed molecular mechanism of this loading process is still elusive. In this study, we demonstrate that the previously uncharacterized C-terminal domain of human Mcm6 is the Cdt1 binding domain (CBD) and present its high resolution NMR structure. The structure of CBD exhibits a typical "winged helix" fold that is generally involved in protein-nucleic acid interaction. Nevertheless, the CBD failed to interact with DNA in our studies, indicating that it is specific for protein-protein interaction. The CBD-Cdt1 interaction involves the helix-turn-helix motif of CBD. The results reported here provide insight into the molecular mechanism of Mcm2-7 chromatin loading and prereplicative complex assembly.
Characterization and structure determination of the Cdt1 binding domain of human minichromosome maintenance (Mcm) 6.,Wei Z, Liu C, Wu X, Xu N, Zhou B, Liang C, Zhu G J Biol Chem. 2010 Apr 23;285(17):12469-73. Epub 2010 Mar 4. PMID:20202939[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ishimi Y. A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex. J Biol Chem. 1997 Sep 26;272(39):24508-13. PMID:9305914
- ↑ Wei Z, Liu C, Wu X, Xu N, Zhou B, Liang C, Zhu G. Characterization and structure determination of the Cdt1 binding domain of human minichromosome maintenance (Mcm) 6. J Biol Chem. 2010 Apr 23;285(17):12469-73. Epub 2010 Mar 4. PMID:20202939 doi:10.1074/jbc.C109.094599
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