 |
PDBsum entry 2c5r
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
DNA-binding protein/DNA
|
PDB id
|
|
|
|
2c5r
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural basis for membrane anchorage of viral phi29 DNA during replication.
|
|
|
Authors
|
|
A.Albert,
D.Muñoz-Espín,
M.Jiménez,
J.L.Asensio,
J.A.Hermoso,
M.Salas,
W.J.Meijer.
|
|
|
Ref.
|
|
J Biol Chem, 2005,
280,
42486-42488.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
|
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.
|
|
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.
|
|
|
|
|
|
The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
42486-42488)
copyright 2005.
|
|
|
|
|
|
|
