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PDBsum entry 2c5r
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DNA-binding protein/DNA
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PDB id
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2c5r
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PDB id:
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| Name: |
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DNA-binding protein/DNA
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Title:
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The structure of phage phi29 replication organizer protein p16.7 in complex with double stranded DNA
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Structure:
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Early protein p16.7. Chain: a, b, c, d, e, f. Fragment: residues 64-130. Engineered: yes. Other_details: dsdna and ssdna binding protein. 5'-d( Tp Cp Cp Ap Cp Cp Gp Gp)-3'. Chain: y. Engineered: yes. 5'-d( Cp Cp Gp Gp Tp Gp Gp Ap)-3'.
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Source:
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Bacillus phage phi29. Organism_taxid: 10756. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic: yes
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Biol. unit:
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Octamer (from PDB file)
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Resolution:
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2.90Å
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R-factor:
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0.254
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R-free:
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0.292
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Authors:
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A.Albert,M.Jimenez,D.Munoz-Espin,J.L.Asensio,J.A.Hermoso,M.Salas, W.J.J.Meijer
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Key ref:
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A.Albert
et al.
(2005).
Structural basis for membrane anchorage of viral phi29 DNA during replication.
J Biol Chem,
280,
42486-42488.
PubMed id:
DOI:
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Date:
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31-Oct-05
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Release date:
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08-Nov-05
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PROCHECK
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Headers
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References
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P16517
(GP167_BPPH2) -
DNA replication protein 16.7 from Bacillus phage phi29
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Seq:
Struc:
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130 a.a.
64 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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T-C-C-A-C-C-G-G
8 bases
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C-C-G-G-T-G-G-A
8 bases
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DOI no:
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J Biol Chem
280:42486-42488
(2005)
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PubMed id:
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Structural basis for membrane anchorage of viral phi29 DNA during replication.
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A.Albert,
D.Muñoz-Espín,
M.Jiménez,
J.L.Asensio,
J.A.Hermoso,
M.Salas,
W.J.Meijer.
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ABSTRACT
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Prokaryotic DNA replication is compartmentalized at the cellular membrane.
Functional and biochemical studies showed that the Bacillus subtilis phage
29-encoded membrane protein p16.7 is directly involved in the organization of
membrane-associated viral DNA replication. The structure of the functional
domain of p16.7 in complex with DNA, presented here, reveals the multimerization
mode of the protein and provides insights in the organization of the phage
genome at the membrane of the infected cell.
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Selected figure(s)
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Figure 2.
Molecular surface representations of a tridimeric p16.7C
unit. A, electrostatic potential (blue, positive and red,
negative). B, positive charged and hydrogen bonding donor side
chains are colored in blue; DNA is schematically displayed.
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Figure 3.
Model of the protein p16.7 anchored to the bacterial
membrane. Residues 1–20 can be modeled as a single
transmembrane helix (not displayed) and residues 30–60 as a
coiled-coil structure.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
42486-42488)
copyright 2005.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.Muñoz-Espín,
R.Daniel,
Y.Kawai,
R.Carballido-López,
V.Castilla-Llorente,
J.Errington,
W.J.Meijer,
and
M.Salas
(2009).
The actin-like MreB cytoskeleton organizes viral DNA replication in bacteria.
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Proc Natl Acad Sci U S A,
(),
0.
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M.Alcorlo,
V.González-Huici,
J.M.Hermoso,
W.J.Meijer,
and
M.Salas
(2007).
The phage phi29 membrane protein p16.7, involved in DNA replication, is required for efficient ejection of the viral genome.
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J Bacteriol,
189,
5542-5549.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
