 |
PDBsum entry 3vu3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxidoreductase/RNA binding protein
|
PDB id
|
|
|
|
3vu3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
727 a.a.
|
|
|
|
|
|
|
|
|
|
|
(+ 0 more)
63 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Oxidoreductase/RNA binding protein
|
|
|
Title:
|
|
Crystal structure of the hfq and catalase hpii complex
|
|
Structure:
|
|
Catalase hpii. Chain: a. Synonym: hydroxyperoxidase ii. Protein hfq. Chain: c, d, e, f, g, h. Synonym: hf-1, host factor-i protein, hf-i
|
|
Source:
|
|
Escherichia coli. Organism_taxid: 83333. Strain: k12. Strain: k12
|
|
Resolution:
|
|
|
2.85Å
|
R-factor:
|
0.199
|
R-free:
|
0.246
|
|
|
Authors:
|
|
M.Watanabe,K.Yonekura
|
|
Key ref:
|
|
K.Yonekura
et al.
(2013).
Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.
Plos One,
8,
e78216.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
15-Jun-12
|
Release date:
|
20-Nov-13
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
Chain A:
E.C.1.11.1.6
- catalase.
|
|
|
|
|
|
|
Reaction:
|
|
2 H2O2 = O2 + 2 H2O
|
|
|
|
|
|
2
×
H2O2
|
=
|
O2
|
+
|
2
×
H2O
|
|
|
|
|
|
|
|
|
|
Cofactor:
|
|
Heme; Mn(2+)
|
|
|
|
|
|
Heme
Bound ligand (Het Group name =
HEM)
matches with 95.45% similarity
|
Mn(2+)
|
|
|
|
|
|
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
| |
|
DOI no:
|
Plos One
8:e78216
(2013)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.
|
|
K.Yonekura,
M.Watanabe,
Y.Kageyama,
K.Hirata,
M.Yamamoto,
S.Maki-Yonekura.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
We report a crystal structure of Hfq and catalase HPII from Escherichia coli.
The post-transcriptional regulator Hfq plays a key role in the survival of
bacteria under stress. A small non-coding RNA (sRNA) DsrA is required for
translation of the stationary phase sigma factor RpoS, which is the central
regulator of the general stress response. Hfq facilitates efficient translation
of rpoS mRNA, which encodes RpoS. Hfq helps in the function of other specific
proteins involved in RNA processing, indicating its versatility in the cell.
However, structural information regarding its interactions with partners is
missing. Here we obtained crystals of Hfq and HPII complexes from cell lysates
following attempts to overexpress a foreign membrane protein. HPII is one of two
catalases in E. coli and its mRNA is transcribed by an RNA polymerase holoenzyme
containing RpoS, which in turn is under positive control of small non-coding
RNAs and of the RNA chaperone Hfq. This sigma factor is known to have a
pronounced effect on the expression of HPII. The crystal structure reveals that
a Hfq hexamer binds each subunit of a HPII tetramer. Each subunit of the Hfq
hexamer exhibits a unique binding mode with HPII. The hexamer of Hfq interacts
via its distal surface. The proximal and distal surfaces are known to
specifically bind different sRNAs, and binding of HPII could affect Hfq
function. Hfq-HPII complexation has no effect on catalase HPII activity.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
|
Links
