1ntc: Difference between revisions
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[[Image:1ntc.jpg|left|200px]] | [[Image:1ntc.jpg|left|200px]] | ||
'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF NTRC WITH THREE ALANINE SUBSTITUTIONS''' | {{Structure | ||
|PDB= 1ntc |SIZE=350|CAPTION= <scene name='initialview01'>1ntc</scene> | |||
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'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF NTRC WITH THREE ALANINE SUBSTITUTIONS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NTC is a [ | 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]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10512705 10512705] | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Pelton, J G.]] | [[Category: Pelton, J G.]] | ||
[[Category: Wemmer, D E.]] | [[Category: Wemmer, D E.]] | ||
[[Category: | [[Category: fi]] | ||
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:28 2008'' | ||
Revision as of 11:01, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF NTRC WITH THREE ALANINE SUBSTITUTIONS
Overview
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.
About this Structure
1NTC is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic 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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