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PDBsum entry 1paa
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Transcription regulation
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PDB id
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1paa
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
33:4460-4470
(1994)
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PubMed id:
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Structure of a histidine-X4-histidine zinc finger domain: insights into ADR1-UAS1 protein-DNA recognition.
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B.E.Bernstein,
R.C.Hoffman,
S.Horvath,
J.R.Herriott,
R.E.Klevit.
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ABSTRACT
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The solution structure for a mutant zinc finger peptide based on the sequence of
the C-terminal ADR1 finger has been determined by two-dimensional NMR
spectroscopy. The mutant peptide, called PAPA, has both proline residues from
the wild-type sequence replaced with alanines. A nonessential cysteine was also
replaced with alanine. The behavior of PAPA in solution implicates the prolines
in the conformational heterogeneity reported earlier for the wild-type peptide
[Xu, R. X., Horvath, S. J., & Klevit, R. E. (1991) Biochemistry 30,
3365-3371]. The solution structure of PAPA reveals several interesting features
of the zinc finger motif. The residue immediately following the second cysteine
ligand adopts a positive phi angle, which we propose is a common feature of this
class of zinc fingers, regardless of whether this residue is a glycine. The NMR
spectrum and resulting solution structure of PAPA suggest that a side-chain to
side-chain hydrogen bond involving an arginine and an aspartic acid analogous to
one observed in the Zif268 protein-DNA cocrystal structure exists in solution in
the absence of DNA [Pavletich, N. P., & Pabo, C. O. (1991) Science 252,
809-817]. A model for the interaction between the two ADR1 zinc fingers and
their DNA binding sites was built by superpositioning the refined solution
structures of PAPA and ADR1b onto the Zif268 structure. This model offers
structural explanations for a variety of mutations to the ADR1 zinc finger
domains that have been shown to affect DNA-binding affinity or specificity.
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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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E.Kellenberger,
C.Dominguez,
S.Fribourg,
E.Wasielewski,
D.Moras,
A.Poterszman,
R.Boelens,
and
B.Kieffer
(2005).
Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions.
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J Biol Chem,
280,
20785-20792.
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PDB code:
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E.Merithew,
C.Stone,
S.Eathiraj,
and
D.G.Lambright
(2003).
Determinants of Rab5 interaction with the N terminus of early endosome antigen 1.
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J Biol Chem,
278,
8494-8500.
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M.Thompson,
and
N.W.Woodbury
(2000).
Fluorescent and photochemical properties of a single zinc finger conjugated to a fluorescent DNA-binding probe.
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Biochemistry,
39,
4327-4338.
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M.Schmiedeskamp,
P.Rajagopal,
and
R.E.Klevit
(1997).
NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1.
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Protein Sci,
6,
1835-1848.
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M.Schmiedeskamp,
and
R.E.Klevit
(1997).
Paramagnetic cobalt as a probe of the orientation of an accessory DNA-binding region of the yeast ADR1 zinc-finger protein.
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Biochemistry,
36,
14003-14011.
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W.D.Kohn,
C.T.Mant,
and
R.S.Hodges
(1997).
Alpha-helical protein assembly motifs.
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J Biol Chem,
272,
2583-2586.
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R.N.Dutnall,
D.Neuhaus,
and
D.Rhodes
(1996).
The solution structure of the first zinc finger domain of SWI5: a novel structural extension to a common fold.
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Structure,
4,
599-611.
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PDB code:
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V.V.Svetlov,
and
T.G.Cooper
(1995).
Review: compilation and characteristics of dedicated transcription factors in Saccharomyces cerevisiae.
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Yeast,
11,
1439-1484.
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B.E.Bernstein,
R.C.Hoffman,
and
R.E.Klevit
(1994).
Sequence-specific DNA recognition by Cys2, His2 zinc fingers.
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Ann N Y Acad Sci,
726,
92.
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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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Links
