1njq
From Proteopedia
(New page: 200px<br /><applet load="1njq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1njq" /> '''NMR structure of the single QALGGH zinc fing...) |
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| - | [[Image:1njq.gif|left|200px]]<br /><applet load="1njq" size=" | + | [[Image:1njq.gif|left|200px]]<br /><applet load="1njq" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR structure of the single QALGGH zinc finger domain from Arabidopsis thaliana SUPERMAN protein'''<br /> | '''NMR structure of the single QALGGH zinc finger domain from Arabidopsis thaliana SUPERMAN protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Zinc finger domains of the classical type represent the most abundant DNA | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1NJQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN, ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1NJQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJQ OCA]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12616630 12616630] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12616630 12616630] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blasio, B | + | [[Category: Blasio, B Di.]] |
[[Category: Bucci, E.]] | [[Category: Bucci, E.]] | ||
[[Category: Digilio, G.]] | [[Category: Digilio, G.]] | ||
| Line 18: | Line 18: | ||
[[Category: Fattorusso, R.]] | [[Category: Fattorusso, R.]] | ||
[[Category: Isernia, C.]] | [[Category: Isernia, C.]] | ||
| - | [[Category: Lello, P | + | [[Category: Lello, P Di.]] |
[[Category: Leone, M.]] | [[Category: Leone, M.]] | ||
[[Category: Pedone, C.]] | [[Category: Pedone, C.]] | ||
| - | [[Category: Pedone, P | + | [[Category: Pedone, P V.]] |
[[Category: Saviano, M.]] | [[Category: Saviano, M.]] | ||
[[Category: Zaccaro, L.]] | [[Category: Zaccaro, L.]] | ||
| Line 31: | Line 31: | ||
[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:53 2008'' |
Revision as of 12:06, 21 February 2008
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NMR structure of the single QALGGH zinc finger domain from Arabidopsis thaliana SUPERMAN protein
Overview
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.
About this Structure
1NJQ is a Single protein structure of sequence from [1] with , and as ligands. Full crystallographic 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 Thu Feb 21 14:06:53 2008
Categories: Single protein | Blasio, B Di. | Bucci, E. | Digilio, G. | Esposito, S. | Fattorusso, R. | Isernia, C. | Lello, P Di. | Leone, M. | Pedone, C. | Pedone, P V. | Saviano, M. | Zaccaro, L. | ACE | NH2 | ZN | Beta-beta-alfa motif | Peptide-zinc complex | Zinc-finger
