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PDBsum entry 1njq
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Metal binding protein
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PDB id
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1njq
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Nmr structure of the single qalggh zinc finger domain from the arabidopsis thaliana superman protein.
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Authors
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C.Isernia,
E.Bucci,
M.Leone,
L.Zaccaro,
P.Di lello,
G.Digilio,
S.Esposito,
M.Saviano,
B.Di blasio,
C.Pedone,
P.V.Pedone,
R.Fattorusso.
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Ref.
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Chembiochem, 2003,
4,
171-180.
[DOI no: ]
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PubMed id
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Abstract
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Zinc finger domains of the classical type represent the most abundant DNA
binding domains in eukaryotic transcription factors. Plant proteins contain from
one to four zinc finger domains, which are characterized by high conservation of
the sequence QALGGH, shown to be critical for DNA-binding activity. The
Arabidopsis thaliana SUPERMAN protein, which contains a single QALGGH zinc
finger, is necessary for proper spatial development of reproductive floral
tissues and has been shown to specifically bind to DNA. Here, we report the
synthesis and UV and NMR spectroscopic structural characterization of a 37 amino
acid SUPERMAN region complexed to a Zn(2+) ion (Zn-SUP37) and present the first
high-resolution structure of a classical zinc finger domain from a plant
protein. The NMR structure of the SUPERMAN zinc finger domain consists of a very
well-defined betabetaalpha motif, typical of all other Cys(2)-His(2) zinc
fingers structurally characterized. As a consequence, the highly conserved
QALGGH sequence is located at the N terminus of the alpha helix. This region of
the domain of animal zinc finger proteins consists of hypervariable residues
that are responsible for recognizing the DNA bases. Therefore, we propose a
peculiar DNA recognition code for the QALGGH zinc finger domain that includes
all or some of the amino acid residues at positions -1, 2, and 3 (numbered
relative to the N terminus of the helix) and possibly others at the C-terminal
end of the recognition helix. This study further confirms that the zinc finger
domain, though very simple, is an extremely versatile DNA binding motif.
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