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protein metals links
Transcription regulation PDB id
1cld
Jmol
Contents
Protein chain
33 a.a. *
Metals
_CD ×2
* Residue conservation analysis
PDB id:
1cld
Name: Transcription regulation
Title: DNA-binding protein
Structure: Cd2-lac9. Chain: a. Engineered: yes. Mutation: yes
Source: Kluyveromyces lactis. Organism_taxid: 28985. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 29 models
Authors: K.H.Gardner,J.E.Coleman
Key ref: K.H.Gardner et al. (1995). Solution structure of the Kluyveromyces lactis LAC9 Cd2 Cys6 DNA-binding domain. Nat Struct Biol, 2, 898-905. PubMed id: 7552715 DOI: 10.1038/nsb1095-898
Date:
06-Jun-95     Release date:   15-Sep-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P08657  (LAC9_KLULA) -  Lactose regulatory protein LAC9
Seq:
Struc: 		 
Seq:
Struc: 		865 a.a.
33 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     regulation of transcription, DNA-dependent   1 term 
  Biochemical function     transcription factor activity     2 terms  

 

 
DOI no: 10.1038/nsb1095-898 Nat Struct Biol 2:898-905 (1995)
PubMed id: 7552715  
 
 
Solution structure of the Kluyveromyces lactis LAC9 Cd2 Cys6 DNA-binding domain.
K.H.Gardner, S.F.Anderson, J.E.Coleman.
 
  ABSTRACT  
 
The Zn2Cys6 DNA-binding domain has been identified by sequence homology in approximately forty fungal proteins, including the K. lactis LAC9 transcriptional activator. Using 1H NMR spectroscopy, we have determined the solution structure of a cadmium-substituted form of the LAC9 DNA-binding domain. We have complemented this approach by applying a series of 113Cd-1H NMR experiments, including several novel heteroTOCSY-based techniques. The DNA-binding domain forms a core of two alpha-helix/extended strand segments around the Cd2 binuclear cluster, with a network of amide proton-cysteinyl S gamma hydrogen bonds stabilizing the cluster. Comparison with other Zn2Cys6 domain structures provides insight into the common structural elements used in metal coordination and DNA binding.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
11266598 G.Marie, L.Serani, O.Laprévote, B.Cahuzac, E.Guittet, and B.Felenbok (2001).
Differential chemical labeling of the AlcR DNA-binding domain from Aspergillas nidulans versus its complex with a 16-mer DNA target: identification of an essential tryptophan involved in the recognition and the interaction with the nucleic acid.
  Protein Sci, 10, 99.  
10617612 A.Hach, T.Hon, and L.Zhang (2000).
The coiled coil dimerization element of the yeast transcriptional activator Hap1, a Gal4 family member, is dispensable for DNA binding but differentially affects transcriptional activation.
  J Biol Chem, 275, 248-254.  
10677209 D.J.Klein, P.E.Johnson, E.S.Zollars, R.N.De Guzman, and M.F.Summers (2000).
The NMR structure of the nucleocapsid protein from the mouse mammary tumor virus reveals unusual folding of the C-terminal zinc knuckle.
  Biochemistry, 39, 1604-1612.
PDB codes: 1dsq 1dsv
10428861 T.Hon, A.Hach, D.Tamalis, Y.Zhu, and L.Zhang (1999).
The yeast heme-responsive transcriptional activator Hap1 is a preexisting dimer in the absence of heme.
  J Biol Chem, 274, 22770-22774.  
  9632766 L.Zhang, A.Hach, and C.Wang (1998).
Molecular mechanism governing heme signaling in yeast: a higher-order complex mediates heme regulation of the transcriptional activator HAP1.
  Mol Cell Biol, 18, 3819-3828.  
  9343383 D.H.Sweet, Y.K.Jang, and G.B.Sancar (1997).
Role of UME6 in transcriptional regulation of a DNA repair gene in Saccharomyces cerevisiae.
  Mol Cell Biol, 17, 6223-6235.  
9118994 R.Näit-Kaoudjt, R.Williams, B.Guiard, and M.Gervais (1997).
Some DNA targets of the yeast CYP1 transcriptional activator are functionally asymmetric--evidence of two half-sites with different affinities.
  Eur J Biochem, 244, 301-309.  
  8887558 L.Zhang, and L.Guarente (1996).
The C6 zinc cluster dictates asymmetric binding by HAP1.
  EMBO J, 15, 4676-4681.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.