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1njq

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[[Image:1njq.gif|left|200px]]
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{{STRUCTURE_1njq| PDB=1njq | SCENE= }}
{{STRUCTURE_1njq| PDB=1njq | SCENE= }}
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'''NMR structure of the single QALGGH zinc finger domain from Arabidopsis thaliana SUPERMAN protein'''
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===NMR structure of the single QALGGH zinc finger domain from Arabidopsis thaliana SUPERMAN protein===
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==Overview==
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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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The line below this paragraph, {{ABSTRACT_PUBMED_12616630}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12616630 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12616630}}
==About this Structure==
==About this Structure==
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1NJQ is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJQ OCA].
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1NJQ is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJQ OCA].
==Reference==
==Reference==
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[[Category: Peptide-zinc complex]]
[[Category: Peptide-zinc complex]]
[[Category: Zinc-finger]]
[[Category: Zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:36:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:44:09 2008''

Revision as of 04:44, 29 July 2008

Image:1njq.png

Template:STRUCTURE 1njq

NMR structure of the single QALGGH zinc finger domain from Arabidopsis thaliana SUPERMAN protein

Template:ABSTRACT PUBMED 12616630

About this Structure

1NJQ is a Single protein structure. Full experimental information is available from OCA.

Reference

NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein., Isernia C, Bucci E, Leone M, Zaccaro L, Di Lello P, Digilio G, Esposito S, Saviano M, Di Blasio B, Pedone C, Pedone PV, Fattorusso R, Chembiochem. 2003 Mar 3;4(2-3):171-80. PMID:12616630

Page seeded by OCA on Tue Jul 29 07:44:09 2008

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