1ntc: Difference between revisions

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[[Image:1ntc.jpg|left|200px]]
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[[Image:1ntc.png|left|200px]]


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{{STRUCTURE_1ntc|  PDB=1ntc  |  SCENE=  }}  
{{STRUCTURE_1ntc|  PDB=1ntc  |  SCENE=  }}  


'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF NTRC WITH THREE ALANINE SUBSTITUTIONS'''
===SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF NTRC WITH THREE ALANINE SUBSTITUTIONS===




==Overview==
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The structure of the 20 kDa C-terminal DNA-binding domain of NtrC from Salmonella typhimurium (residues Asp380-Glu469) with alanine replacing Arg456, Asn457, and Arg461, was determined by NMR spectroscopy. NtrC is a homodimeric enhancer-binding protein that activates the transcription of genes whose products are required for nitrogen metabolism. The 91-residue C-terminal domain contains the determinants necessary for dimerization and DNA-binding of the full length protein. The mutant protein does not bind to DNA but retains many characteristics of the wild-type protein, and the mutant domain expresses at high yield (20 mg/l) in minimal medium. Three-dimensional (1)H/(13)C/(15)N triple-resonance, (1)H-(13)C-(13)C-(1)H correlation and (15)N-separated nuclear Overhauser effect (NOE) spectroscopy experiments were used to make backbone and side-chain (1)H,(15)N, and (13)C assignments. The structures were calculated using a total of 1580 intra and inter-monomer distance and hydrogen bond restraints (88 hydrogen bonds; 44 hydrogen bond restraints), and 88 phi dihedral restraints for residues Asp400 through Glu469 in both monomers. A total of 54 ambiguous restraints (intra or inter-monomer) involving residues close to the 2-fold symmetry axis were also included. Each monomer consists of four helical segments. Helices A (Trp402-Leu414) and B (Leu421-His440) join with those of another monomer to form an antiparallel four-helix bundle. Helices C (Gln446-Leu451) and D (Ala456-Met468) of each monomer adopt a classic helix-turn-helix DNA-binding fold at either end of the protein. The backbone rms deviation for the 28 best of 40 starting structures is 0.6 (+/-0.2) A. Structural differences between the C-terminal domain of NtrC and the homologous Factor for Inversion Stimulation are discussed.
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==About this Structure==
==About this Structure==
1NTC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NTC OCA].  
1NTC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NTC OCA].  


==Reference==
==Reference==
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[[Category: Four-helix bundle]]
[[Category: Four-helix bundle]]
[[Category: Helix-turn-helix]]
[[Category: Helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:32:31 2008''

Revision as of 06:32, 28 July 2008

File:1ntc.png

Template:STRUCTURE 1ntc

SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF NTRC WITH THREE ALANINE SUBSTITUTIONS

Template:ABSTRACT PUBMED 10512705

About this Structure

1NTC is a Single protein structure of sequence from Salmonella typhimurium. Full experimental information is available from OCA.

Reference

Solution structure of the DNA-binding domain of NtrC with three alanine substitutions., Pelton JG, Kustu S, Wemmer DE, J Mol Biol. 1999 Oct 8;292(5):1095-110. PMID:10512705

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