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PDBsum entry 2xrn

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protein Protein-protein interface(s) links
DNA binding protein PDB id
2xrn

 

 

 

 

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Contents
Protein chains
239 a.a. *
Waters ×7
* Residue conservation analysis
PDB id:
2xrn
Name: DNA binding protein
Title: Crystal structure of ttgv
Structure: Hth-type transcriptional regulator ttgv. Chain: a, b. Fragment: residues 14-253. Synonym: toluene tolerance pump ttgghi operon repressor. Engineered: yes. Mutation: yes
Source: Pseudomonas putida. Organism_taxid: 303. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.90Å     R-factor:   0.216     R-free:   0.279
Authors: D.Lu,S.Fillet,C.Meng,Y.Alguel,P.Kloppsteck,J.Bergeron,T.Krell,M.- T.Gallegos,J.Ramos,X.Zhang
Key ref: D.Lu et al. (2010). Crystal structure of TtgV in complex with its DNA operator reveals a general model for cooperative DNA binding of tetrameric gene regulators. Genes Dev, 24, 2556-2565. PubMed id: 21078819
Date:
17-Sep-10     Release date:   01-Dec-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q93PU6  (TTGV_PSEPT) -  HTH-type transcriptional regulator TtgV from Pseudomonas putida (strain DOT-T1E)
Seq:
Struc:
259 a.a.
239 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Genes Dev 24:2556-2565 (2010)
PubMed id: 21078819  
 
 
Crystal structure of TtgV in complex with its DNA operator reveals a general model for cooperative DNA binding of tetrameric gene regulators.
D.Lu, S.Fillet, C.Meng, Y.Alguel, P.Kloppsteck, J.Bergeron, T.Krell, M.T.Gallegos, J.Ramos, X.Zhang.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21502508 J.M.Ortiz-Guerrero, M.C.Polanco, F.J.Murillo, S.Padmanabhan, and M.Elías-Arnanz (2011).
Light-dependent gene regulation by a coenzyme B12-based photoreceptor.
  Proc Natl Acad Sci U S A, 108, 7565-7570.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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