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| | ==Mcm10 C-terminal DNA binding domain== | | ==Mcm10 C-terminal DNA binding domain== |
| - | <StructureSection load='2kwq' size='340' side='right'caption='[[2kwq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kwq' size='340' side='right'caption='[[2kwq]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kwq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KWQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KWQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kwq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KWQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mcm10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2kwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kwq OCA], [http://pdbe.org/2kwq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kwq RCSB], [http://www.ebi.ac.uk/pdbsum/2kwq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kwq ProSAT]</span></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=2kwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kwq OCA], [https://pdbe.org/2kwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kwq RCSB], [https://www.ebi.ac.uk/pdbsum/2kwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kwq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MCM10_XENLA MCM10_XENLA]] Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication (By similarity).<ref>PMID:11864598</ref> | + | [https://www.uniprot.org/uniprot/MCM10_XENLA MCM10_XENLA] Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication (By similarity).<ref>PMID:11864598</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: African clawed frog]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chagot, B]] | + | [[Category: Xenopus laevis]] |
| - | [[Category: Chazin, W J]] | + | [[Category: Chagot B]] |
| - | [[Category: Eichman, B F]]
| + | [[Category: Chazin WJ]] |
| - | [[Category: Robertson, P D]] | + | [[Category: Eichman BF]] |
| - | [[Category: Dna binding]] | + | [[Category: Robertson PD]] |
| - | [[Category: Dna binding protein]] | + | |
| - | [[Category: Dna replication]]
| + | |
| - | [[Category: Mcm10]]
| + | |
| - | [[Category: Zinc motif]]
| + | |
| - | [[Category: Zinc ribbon]]
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| Structural highlights
Function
MCM10_XENLA Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication (By similarity).[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 eukaryotic DNA replication protein Mcm10 associates with chromatin in early S-phase and is required for assembly and function of the replication fork protein machinery. Xenopus laevis (X) Mcm10 binds DNA via a highly conserved internal domain (ID) and a C-terminal domain (CTD) that is unique to higher eukaryotes. Although the structural basis of the interactions of the ID with DNA and polymerase alpha is known, little information is available for the CTD. We have identified the minimal DNA binding region of the XMcm10-CTD and determined its three-dimensional structure by solution NMR. The CTD contains a globular domain composed of two zinc binding motifs. NMR chemical shift perturbation and mutational analysis show that ssDNA binds only to the N-terminal (CCCH-type) zinc motif, whose structure is unique to Mcm10. The second (CCCC-type) zinc motif is not involved in DNA binding. However, it is structurally similar to the CCCC zinc ribbon in the N-terminal oligomerization domain of eukaryotic and archaeal MCM helicases. NMR analysis of a construct spanning both the ID and CTD reveals that the two DNA binding domains are structurally independent in solution, supporting a modular architecture for vertebrate Mcm10. Our results provide insight in the action of Mcm10 in the replisome and support a model in which it serves as a central scaffold through coupling of interactions with partner proteins and the DNA.
Solution NMR structure of the C-terminal DNA binding domain of Mcm10 reveals a conserved MCM motif.,Robertson PD, Chagot B, Chazin WJ, Eichman BF J Biol Chem. 2010 Jul 23;285(30):22942-9. Epub 2010 May 19. PMID:20489205[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wohlschlegel JA, Dhar SK, Prokhorova TA, Dutta A, Walter JC. Xenopus Mcm10 binds to origins of DNA replication after Mcm2-7 and stimulates origin binding of Cdc45. Mol Cell. 2002 Feb;9(2):233-40. PMID:11864598
- ↑ Robertson PD, Chagot B, Chazin WJ, Eichman BF. Solution NMR structure of the C-terminal DNA binding domain of Mcm10 reveals a conserved MCM motif. J Biol Chem. 2010 Jul 23;285(30):22942-9. Epub 2010 May 19. PMID:20489205 doi:10.1074/jbc.M110.131276
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