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PDBsum entry 4pog
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Replication, DNA binding protein/DNA
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PDB id
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4pog
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PDB id:
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| Name: |
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Replication, DNA binding protein/DNA
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Title:
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Mcm-ssdna co-crystal structure
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Structure:
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Cell division control protein 21. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Fragment: n-terminal domain (unp residues 2-256). Synonym: mcm. Engineered: yes. 30-mer oligo(dt). Chain: x, v, y, z. Engineered: yes
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Source:
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Pyrococcus furiosus. Organism_taxid: 186497. Strain: atcc 43587 / dsm 3638 / jcm 8422 / vc1. Gene: cdc21, pf0482. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes
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Resolution:
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3.20Å
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R-factor:
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0.259
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R-free:
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0.294
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Authors:
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C.A.Froelich,S.Kang,L.B.Epling,S.P.Bell,E.J.Enemark
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Key ref:
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C.A.Froelich
et al.
(2014).
A conserved MCM single-stranded DNA binding element is essential for replication initiation.
Elife,
3,
e01993.
PubMed id:
DOI:
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Date:
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25-Feb-14
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Release date:
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09-Apr-14
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PROCHECK
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Headers
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References
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Q8U3I4
(Q8U3I4_PYRFU) -
DNA helicase from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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Seq:
Struc:
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1049 a.a.
255 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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T-T-T-T-T-T-T
7 bases
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T-T-T-T
4 bases
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T-T-T-T-T-T-T-T-T-T-T
11 bases
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T-T-T-T-T-T-T
7 bases
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Enzyme class:
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E.C.3.6.4.12
- Dna helicase.
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Reaction:
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ATP + H2O = ADP + phosphate + H+
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ATP
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+
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H2O
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=
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ADP
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+
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phosphate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Elife
3:e01993
(2014)
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PubMed id:
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A conserved MCM single-stranded DNA binding element is essential for replication initiation.
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C.A.Froelich,
S.Kang,
L.B.Epling,
S.P.Bell,
E.J.Enemark.
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ABSTRACT
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The ring-shaped MCM helicase is essential to all phases of DNA replication. The
complex loads at replication origins as an inactive double-hexamer encircling
duplex DNA. Helicase activation converts this species to two active single
hexamers that encircle single-stranded DNA (ssDNA). The molecular details of MCM
DNA interactions during these events are unknown. We determined the crystal
structure of the Pyrococcus furiosus MCM N-terminal domain hexamer bound to
ssDNA and define a conserved MCM-ssDNA binding motif (MSSB). Intriguingly, ssDNA
binds the MCM ring interior perpendicular to the central channel with defined
polarity. In eukaryotes, the MSSB is conserved in several Mcm2-7 subunits, and
MSSB mutant combinations in S. cerevisiae Mcm2-7 are not viable. Mutant Mcm2-7
complexes assemble and are recruited to replication origins, but are defective
in helicase loading and activation. Our findings identify an important MCM-ssDNA
interaction and suggest it functions during helicase activation to select the
strand for translocation. DOI: http://dx.doi.org/10.7554/eLife.01993.001.
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