 |
PDBsum entry 4zds
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription activator
|
PDB id
|
|
|
|
4zds
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Transcription activator
|
|
|
Title:
|
|
Crystal structure of core DNA binding domain of arabidopsis thaliana transcription factor ethylene-insensitive 3
|
|
Structure:
|
|
Protein ethylene insensitive 3. Chain: a, b. Fragment: unp residues 174-306
|
|
Source:
|
|
Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702
|
|
Resolution:
|
|
|
1.78Å
|
R-factor:
|
0.177
|
R-free:
|
0.218
|
|
|
Authors:
|
|
J.Song,C.Zhu,X.Zhang,X.Wen,L.Liu,J.Peng,H.Guo,C.Yi
|
|
Key ref:
|
|
J.Song
et al.
(2015).
Biochemical and Structural Insights into the Mechanism of DNA Recognition by Arabidopsis ETHYLENE INSENSITIVE3.
Plos One,
10,
e0137439.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
18-Apr-15
|
Release date:
|
23-Sep-15
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
O24606
(EIN3_ARATH) -
Protein ETHYLENE INSENSITIVE 3 from Arabidopsis thaliana
|
|
|
|
Seq:
Struc:
|
|
|
|
628 a.a.
132 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Plos One
10:e0137439
(2015)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Biochemical and Structural Insights into the Mechanism of DNA Recognition by Arabidopsis ETHYLENE INSENSITIVE3.
|
|
J.Song,
C.Zhu,
X.Zhang,
X.Wen,
L.Liu,
J.Peng,
H.Guo,
C.Yi.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Gaseous hormone ethylene regulates numerous stress responses and developmental
adaptations in plants by controlling gene expression via transcription factors
ETHYLENE INSENSITIVE3 (EIN3) and EIN3-Like1 (EIL1). However, our knowledge
regarding to the accurate definition of DNA-binding domains (DBDs) within EIN3
and also the mechanism of specific DNA recognition by EIN3 is limited. Here, we
identify EIN3 82-352 and 174-306 as the optimal and core DBDs, respectively.
Results from systematic biochemical analyses reveal that both the number of
EIN3-binding sites (EBSs) and the spacing length between two EBSs affect the
binding affinity of EIN3; accordingly, a new DNA probe which has higher affinity
with EIN3 than ERF1 is also designed. Furthermore, we show that palindromic
repeat sequences in ERF1 promoter are not necessary for EIN3 binding. Finally,
we provide, to our knowledge, the first crystal structure of EIN3 core DBD,
which contains amino acid residues essential for DNA binding and signaling.
Collectively, these data suggest the detailed mechanism of DNA recognition by
EIN3 and provide an in-depth view at molecular level for the transcriptional
regulation mediated by EIN3.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
