 |
PDBsum entry 5jrj
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
DNA binding protein
|
PDB id
|
|
|
|
5jrj
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
DNA binding protein
|
|
|
Title:
|
|
Crystal structure of herbaspirillum seropedicae reca
|
|
Structure:
|
|
Protein reca. Chain: a. Synonym: recombinase a. Engineered: yes
|
|
Source:
|
|
Herbaspirillum seropedicae. Organism_taxid: 964. Strain: smr1. Cell: proteobacteria. Gene: reca. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
Resolution:
|
|
|
1.70Å
|
R-factor:
|
0.177
|
R-free:
|
0.211
|
|
|
Authors:
|
|
W.C.Leite,C.W.Galvao,S.C.Saab,J.Iulek,R.M.Etto,M.B.R.Steffens, S.Chitteni-Pattu,T.Stanage,J.L.Keck,M.M.Cox
|
|
Key ref:
|
|
W.C.Leite
et al.
(2016).
Structural and Functional Studies of H. seropedicae RecA Protein - Insights into the Polymerization of RecA Protein as Nucleoprotein Filament.
PLoS One,
11,
e0159871.
PubMed id:
|
|
|
Date:
|
|
|
06-May-16
|
Release date:
|
03-Aug-16
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
D8IYL4
(D8IYL4_HERSS) -
Protein RecA from Herbaspirillum seropedicae (strain SmR1)
|
|
|
|
Seq:
Struc:
|
|
|
|
351 a.a.
306 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
PLoS One
11:e0159871
(2016)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structural and Functional Studies of H. seropedicae RecA Protein - Insights into the Polymerization of RecA Protein as Nucleoprotein Filament.
|
|
W.C.Leite,
C.W.Galvão,
S.C.Saab,
J.Iulek,
R.M.Etto,
M.B.Steffens,
S.Chitteni-Pattu,
T.Stanage,
J.L.Keck,
M.M.Cox.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The bacterial RecA protein plays a role in the complex system of DNA damage
repair. Here, we report the functional and structural characterization of the
Herbaspirillum seropedicae RecA protein (HsRecA). HsRecA protein is more
efficient at displacing SSB protein from ssDNA than Escherichia coli RecA
protein. HsRecA also promotes DNA strand exchange more efficiently. The three
dimensional structure of HsRecA-ADP/ATP complex has been solved to 1.7 Å
resolution. HsRecA protein contains a small N-terminal domain, a central core
ATPase domain and a large C-terminal domain, that are similar to homologous
bacterial RecA proteins. Comparative structural analysis showed that the
N-terminal polymerization motif of archaeal and eukaryotic RecA family proteins
are also present in bacterial RecAs. Reconstruction of electrostatic potential
from the hexameric structure of HsRecA-ADP/ATP revealed a high positive charge
along the inner side, where ssDNA is bound inside the filament. The properties
of this surface may explain the greater capacity of HsRecA protein to bind
ssDNA, forming a contiguous nucleoprotein filament, displace SSB and promote DNA
exchange relative to EcRecA. Our functional and structural analyses provide
insight into the molecular mechanisms of polymerization of bacterial RecA as a
helical nucleoprotein filament.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
