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Transcription regulation
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PDB id
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1ajy
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Contents |
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* Residue conservation analysis
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PDB id:
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Transcription regulation
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Title:
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Structure and mobility of the put3 dimer: a DNA pincer, nmr, 13 structures
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Structure:
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Put3. Chain: a, b. Fragment: DNA-binding domain, residues 31 - 100
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Other_details: expressed in escherichia coli
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NMR struc:
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13 models
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Authors:
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K.J.Walters,K.T.Dayie,R.J.Reece,M.Ptashne,G.Wagner
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Key ref:
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K.J.Walters
et al.
(1997).
Structure and mobility of the PUT3 dimer.
Nat Struct Biol,
4,
744-750.
PubMed id:
DOI:
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Date:
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12-May-97
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Release date:
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17-Sep-97
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PROCHECK
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Headers
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References
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P25502
(PUT3_YEAST) -
Proline utilization trans-activator
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Seq: Struc:
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979 a.a.
71 a.a.*
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Key: |
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PfamA domain |
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PfamB domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Gene Ontology (GO) functional annotation
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Cellular component
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nucleus
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1 term
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Biological process
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regulation of transcription, DNA-dependent
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1 term
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Biochemical function
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transcription factor activity
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2 terms
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DOI no:
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Nat Struct Biol
4:744-750
(1997)
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PubMed id:
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Structure and mobility of the PUT3 dimer.
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K.J.Walters,
K.T.Dayie,
R.J.Reece,
M.Ptashne,
G.Wagner.
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ABSTRACT
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The solution structure and backbone dynamics of the transcriptional activator
PUT3 (31-100) has been characterized using NMR spectroscopy. PUT3 (31-100)
contains three distinct domains: a cysteine zinc cluster, linker, and
dimerization domain. The cysteine zinc cluster of PUT3 closely resembles the
solution structure of GAL4, while the dimerization domain forms a long
coiled-coil similar to that observed in the crystal structures of GAL4 and PPR1.
However, the residues at the N-terminal end of the coiled-coil behave very
differently in each of these proteins. A comparison of the structural elements
within this region provides a model for the DNA binding specificity of these
proteins. Furthermore, we have characterized the dynamics of PUT3 to find that
the zinc cluster and dimerization domains have very diverse dynamics in
solution. The dimerization domain behaves as a large protein, while the
peripheral cysteine zinc clusters have dynamic properties similar to small
proteins.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.MacPherson,
M.Larochelle,
and
B.Turcotte
(2006).
A fungal family of transcriptional regulators: the zinc cluster proteins.
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Microbiol Mol Biol Rev, 70,
583-604.
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K.F.Kubatzky,
W.Liu,
K.Goldgraben,
C.Simmerling,
S.O.Smith,
and
S.N.Constantinescu
(2005).
Structural requirements of the extracellular to transmembrane domain junction for erythropoietin receptor function.
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J Biol Chem, 280,
14844-14854.
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B.Akache,
S.MacPherson,
M.A.Sylvain,
and
B.Turcotte
(2004).
Complex interplay among regulators of drug resistance genes in Saccharomyces cerevisiae.
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J Biol Chem, 279,
27855-27860.
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C.A.Sellick,
and
R.J.Reece
(2003).
Modulation of transcription factor function by an amino acid: activation of Put3p by proline.
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EMBO J, 22,
5147-5153.
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X.Wang,
C.F.Basler,
B.R.Williams,
R.H.Silverman,
P.Palese,
and
A.García-Sastre
(2002).
Functional replacement of the carboxy-terminal two-thirds of the influenza A virus NS1 protein with short heterologous dimerization domains.
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J Virol, 76,
12951-12962.
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P.Hidalgo,
A.Z.Ansari,
P.Schmidt,
B.Hare,
N.Simkovich,
S.Farrell,
E.J.Shin,
M.Ptashne,
and
G.Wagner
(2001).
Recruitment of the transcriptional machinery through GAL11P: structure and interactions of the GAL4 dimerization domain.
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Genes Dev, 15,
1007-1020.
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PDB code:
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H.L.Huang,
and
M.C.Brandriss
(2000).
The regulator of the yeast proline utilization pathway is differentially phosphorylated in response to the quality of the nitrogen source.
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Mol Cell Biol, 20,
892-899.
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M.D'Alessio,
and
M.C.Brandriss
(2000).
Cross-pathway regulation in Saccharomyces cerevisiae: activation of the proline utilization pathway by Ga14p in vivo.
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J Bacteriol, 182,
3748-3753.
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I.Nikolaev,
F.Lenouvel,
and
B.Felenbok
(1999).
Unique DNA binding specificity of the binuclear zinc AlcR activator of the ethanol utilization pathway in Aspergillus nidulans.
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J Biol Chem, 274,
9795-9802.
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P.C.Liu,
and
D.J.Thiele
(1999).
Modulation of human heat shock factor trimerization by the linker domain.
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J Biol Chem, 274,
17219-17225.
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Z.Y.Sun,
V.Dötsch,
M.Kim,
J.Li,
E.L.Reinherz,
and
G.Wagner
(1999).
Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies.
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EMBO J, 18,
2941-2949.
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PDB code:
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J.Noël,
and
B.Turcotte
(1998).
Zinc cluster proteins Leu3p and Uga3p recognize highly related but distinct DNA targets.
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J Biol Chem, 273,
17463-17468.
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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
code is
shown on the right.
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