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PDBsum entry 2ebi

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protein links
DNA binding protein PDB id
2ebi
Jmol
Contents
Protein chain
86 a.a. *
* Residue conservation analysis
PDB id:
2ebi
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: 20717979
Date:
08-Feb-07     Release date:   19-Feb-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9FX53  (TGT1_ARATH) -  Trihelix transcription factor GT-1
Seq:
Struc:
406 a.a.
86 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     transcription, DNA-dependent   1 term 
  Biochemical function     chromatin binding     3 terms  

 

 
Proteins 78:3033-3047 (2010)
PubMed id: 20717979  
 
 
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  
 
No abstract given.