6rax

From Proteopedia

(Difference between revisions)

Current revision

D. melanogaster CMG-DNA, State 1B

6rax, resolution 3.99Å

Structural highlights

6rax is a 13 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	Mcm2, CG7538 (DROME), Psf1, CG9187-PA, Dmel\CG9187, psf1, CG9187, Dmel_CG9187 (DROME), Psf2, CG18013 (DROME), Psf3, Dmel\CG2222, CG2222, Dmel_CG2222 (DROME), Sld5, anon-WO0172774.61, Dmel\CG14549, CG14549, Dmel_CG14549 (DROME), Mcm3, Mcm3-RA, CG4206 (DROME), dpa, CG1616 (DROME), Mcm5, CG4082 (DROME), Mcm6, CG4039 (DROME), Mcm7, CG4978 (DROME), CDC45L, anon-1Ec, CDC45, Cdc45, cdc45, D, dCDC45, dCDC45L, DmCdc45, Dmel\CG3658, EG:BACR7A4.11, CG3658, Dmel_CG3658 (DROME)
Activity:	DNA helicase, with EC number 3.6.4.12
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MCM7_DROME] 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] ^[2] [PSF2_DROME] The GINS complex plays an essential role in the initiation of DNA replication. [MCM4_DROME] 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 DNA replication and cell proliferation. Essential role in mitotic DNA replication but not in endoreplication.^[3] ^[4] [MCM3_DROME] Acts as component of the Mcm2-7 complex (Mcm 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.^[5] ^[6] [MCM2_DROME] 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 DNA replication and cell proliferation.^[7] ^[8] ^[9] [MCM5_DROME] 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.^[10] ^[11] [Q9VBI1_DROME] The GINS complex plays an essential role in the initiation of DNA replication.[PIRNR:PIRNR007764] [MCM6_DROME] 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 DNA replication and cell proliferation. Required for mitotic cycles, endocycles, and the special S phase associated with the amplification of chorion genes; has a role in origin unwinding or fork elongation at chorion loci.^[12] ^[13] ^[14]

Publication Abstract from PubMed

In the eukaryotic replisome, DNA unwinding by the Cdc45-MCM-Go-Ichi-Ni-San (GINS) (CMG) helicase requires a hexameric ring-shaped ATPase named minichromosome maintenance (MCM), which spools single-stranded DNA through its central channel. Not all six ATPase sites are required for unwinding; however, the helicase mechanism is unknown. We imaged ATP-hydrolysis-driven translocation of the CMG using cryo-electron microscopy (cryo-EM) and found that the six MCM subunits engage DNA using four neighboring protomers at a time, with ATP binding promoting DNA engagement. Morphing between different helicase states leads us to suggest a non-symmetric hand-over-hand rotary mechanism, explaining the asymmetric requirements of ATPase function around the MCM ring of the CMG. By imaging of a higher-order replisome assembly, we find that the Mrc1-Csm3-Tof1 fork-stabilization complex strengthens the interaction between parental duplex DNA and the CMG at the fork, which might support the coupling between DNA translocation and fork unwinding.

Molecular Basis for ATP-Hydrolysis-Driven DNA Translocation by the CMG Helicase of the Eukaryotic Replisome.,Eickhoff P, Kose HB, Martino F, Petojevic T, Abid Ali F, Locke J, Tamberg N, Nans A, Berger JM, Botchan MR, Yardimci H, Costa A Cell Rep. 2019 Sep 3;28(10):2673-2688.e8. doi: 10.1016/j.celrep.2019.07.104. PMID:31484077^[15]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Moyer SE, Lewis PW, Botchan MR. Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase. Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10236-10241. doi:, 10.1073/pnas.0602400103. Epub 2006 Jun 23. PMID:16798881 doi:http://dx.doi.org/10.1073/pnas.0602400103
↑ Ilves I, Petojevic T, Pesavento JJ, Botchan MR. Activation of the MCM2-7 Helicase by Association with Cdc45 and GINS Proteins. Mol Cell. 2010 Jan 29;37(2):247-258. PMID:20122406 doi:http://dx.doi.org/S1097-2765(09)00963-0
↑ Moyer SE, Lewis PW, Botchan MR. Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase. Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10236-10241. doi:, 10.1073/pnas.0602400103. Epub 2006 Jun 23. PMID:16798881 doi:http://dx.doi.org/10.1073/pnas.0602400103
↑ Ilves I, Petojevic T, Pesavento JJ, Botchan MR. Activation of the MCM2-7 Helicase by Association with Cdc45 and GINS Proteins. Mol Cell. 2010 Jan 29;37(2):247-258. PMID:20122406 doi:http://dx.doi.org/S1097-2765(09)00963-0
↑ Moyer SE, Lewis PW, Botchan MR. Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase. Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10236-10241. doi:, 10.1073/pnas.0602400103. Epub 2006 Jun 23. PMID:16798881 doi:http://dx.doi.org/10.1073/pnas.0602400103
↑ Ilves I, Petojevic T, Pesavento JJ, Botchan MR. Activation of the MCM2-7 Helicase by Association with Cdc45 and GINS Proteins. Mol Cell. 2010 Jan 29;37(2):247-258. PMID:20122406 doi:http://dx.doi.org/S1097-2765(09)00963-0
↑ Moyer SE, Lewis PW, Botchan MR. Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase. Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10236-10241. doi:, 10.1073/pnas.0602400103. Epub 2006 Jun 23. PMID:16798881 doi:http://dx.doi.org/10.1073/pnas.0602400103
↑ Ilves I, Petojevic T, Pesavento JJ, Botchan MR. Activation of the MCM2-7 Helicase by Association with Cdc45 and GINS Proteins. Mol Cell. 2010 Jan 29;37(2):247-258. PMID:20122406 doi:http://dx.doi.org/S1097-2765(09)00963-0
↑ Treisman JE, Follette PJ, O'Farrell PH, Rubin GM. Cell proliferation and DNA replication defects in a Drosophila MCM2 mutant. Genes Dev. 1995 Jul 15;9(14):1709-15. PMID:7622035
↑ Moyer SE, Lewis PW, Botchan MR. Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase. Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10236-10241. doi:, 10.1073/pnas.0602400103. Epub 2006 Jun 23. PMID:16798881 doi:http://dx.doi.org/10.1073/pnas.0602400103
↑ Ilves I, Petojevic T, Pesavento JJ, Botchan MR. Activation of the MCM2-7 Helicase by Association with Cdc45 and GINS Proteins. Mol Cell. 2010 Jan 29;37(2):247-258. PMID:20122406 doi:http://dx.doi.org/S1097-2765(09)00963-0
↑ Schwed G, May N, Pechersky Y, Calvi BR. Drosophila minichromosome maintenance 6 is required for chorion gene amplification and genomic replication. Mol Biol Cell. 2002 Feb;13(2):607-20. doi: 10.1091/mbc.01-08-0400. PMID:11854416 doi:http://dx.doi.org/10.1091/mbc.01-08-0400
↑ Moyer SE, Lewis PW, Botchan MR. Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase. Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10236-10241. doi:, 10.1073/pnas.0602400103. Epub 2006 Jun 23. PMID:16798881 doi:http://dx.doi.org/10.1073/pnas.0602400103
↑ Ilves I, Petojevic T, Pesavento JJ, Botchan MR. Activation of the MCM2-7 Helicase by Association with Cdc45 and GINS Proteins. Mol Cell. 2010 Jan 29;37(2):247-258. PMID:20122406 doi:http://dx.doi.org/S1097-2765(09)00963-0
↑ Eickhoff P, Kose HB, Martino F, Petojevic T, Abid Ali F, Locke J, Tamberg N, Nans A, Berger JM, Botchan MR, Yardimci H, Costa A. Molecular Basis for ATP-Hydrolysis-Driven DNA Translocation by the CMG Helicase of the Eukaryotic Replisome. Cell Rep. 2019 Sep 3;28(10):2673-2688.e8. doi: 10.1016/j.celrep.2019.07.104. PMID:31484077 doi:http://dx.doi.org/10.1016/j.celrep.2019.07.104

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6rax"

@@ Line 3: / Line 3: @@
 <SX load='6rax' size='340' side='right' viewer='molstar' caption='[[6rax]], [[Resolution|resolution]] 3.99&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6rax]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RAX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6rax]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RAX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RAX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mcm2, CG7538 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Psf1, CG9187-PA, Dmel\CG9187, psf1, CG9187, Dmel_CG9187 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Psf2, CG18013 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Psf3, Dmel\CG2222, CG2222, Dmel_CG2222 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Sld5, anon-WO0172774.61, Dmel\CG14549, CG14549, Dmel_CG14549 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Mcm3, Mcm3-RA, CG4206 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), dpa, CG1616 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Mcm5, CG4082 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Mcm6, CG4039 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Mcm7, CG4978 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), CDC45L, anon-1Ec, CDC45, Cdc45, cdc45, D, dCDC45, dCDC45L, DmCdc45, Dmel\CG3658, EG:BACR7A4.11, CG3658, Dmel_CG3658 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
 <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>
-<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=6rax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rax OCA], [http://pdbe.org/6rax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rax RCSB], [http://www.ebi.ac.uk/pdbsum/6rax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rax ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rax OCA], [http://pdbe.org/6rax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rax RCSB], [http://www.ebi.ac.uk/pdbsum/6rax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rax ProSAT]</span></td></tr>
 </table>
 == Function ==

6rax

From Proteopedia

Current revision

D. melanogaster CMG-DNA, State 1B

Structural highlights

Function

Publication Abstract from PubMed

References

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