 |
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
DNA binding protein
|
PDB id
|
|
|
|
2ebi
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
DNA binding protein
|
 |
|
Title:
|
 |
Arabidopsis gt-1 DNA-binding domain with t133d phosphomimeti
|
|
Structure:
|
 |
DNA binding protein gt-1. Chain: a. Fragment: DNA-binding domain, residues 81-166. Synonym: hypothetical protein at1g13450. Engineered: yes. Mutation: yes
|
|
Source:
|
 |
Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: t6j4.18. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
NMR struc:
|
 |
20 models
|
 |
|
Authors:
|
 |
T.Nagata,K.Noto,E.Niyada,Y.Ikeda,Y.Yamamoto,S.Uesugi,J.Murat K.Hiratsuka,M.Katahira
|
|
Key ref:
|
 |
T.Nagata
et al.
(2010).
Solution structures of the trihelix DNA-binding domains of the wild-type and a phosphomimetic mutant of Arabidopsis GT-1: mechanism for an increase in DNA-binding affinity through phosphorylation.
Proteins,
78,
3033-3047.
PubMed id:
DOI:
|
 |
|
Date:
|
 |
|
08-Feb-07
|
Release date:
|
19-Feb-08
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
Q9FX53
(TGT1_ARATH) -
Trihelix transcription factor GT-1
|
|
|
|
Seq: Struc:
|
 |
 |
 |
406 a.a.
86 a.a.*
|
|
|
|
|
|
|
 |
 |
|
|
Key: |
 |
PfamA domain |
 |
 |
PfamB domain |
 |
 |
 |
Secondary structure |
 |
|
*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
|
|
|
|
|
 |
|
 |
|
 |
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
 |
 |
 |
|
 |
 |
 |
 |
|
 |
|
Biological process
|
regulation of transcription
|
1 term
|
 |
|
Biochemical function
|
DNA binding
|
1 term
|
 |
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
Proteins
78:3033-3047
(2010)
|
|
PubMed id:
|
|
|
|
|
| |
|
Solution structures of the trihelix DNA-binding domains of the wild-type and a phosphomimetic mutant of Arabidopsis GT-1: mechanism for an increase in DNA-binding affinity through phosphorylation.
|
|
T.Nagata,
E.Niyada,
N.Fujimoto,
Y.Nagasaki,
K.Noto,
Y.Miyanoiri,
J.Murata,
K.Hiratsuka,
M.Katahira.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
|