1cey: Difference between revisions
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'''ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF CHEMOTAXIS Y PROTEIN USING THREE-AND FOUR-DIMENSIONAL HETERONUCLEAR (13C,15N) NMR SPECTROSCOPY''' | {{Structure | ||
|PDB= 1cey |SIZE=350|CAPTION= <scene name='initialview01'>1cey</scene> | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF CHEMOTAXIS Y PROTEIN USING THREE-AND FOUR-DIMENSIONAL HETERONUCLEAR (13C,15N) NMR SPECTROSCOPY''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CEY is a [ | 1CEY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEY OCA]. | ||
==Reference== | ==Reference== | ||
Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy., Moy FJ, Lowry DF, Matsumura P, Dahlquist FW, Krywko JE, Domaille PJ, Biochemistry. 1994 Sep 6;33(35):10731-42. PMID:[http:// | Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy., Moy FJ, Lowry DF, Matsumura P, Dahlquist FW, Krywko JE, Domaille PJ, Biochemistry. 1994 Sep 6;33(35):10731-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8075074 8075074] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
''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 10:23:33 2008'' | ||
Revision as of 08:23, 20 March 2008
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ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF CHEMOTAXIS Y PROTEIN USING THREE-AND FOUR-DIMENSIONAL HETERONUCLEAR (13C,15N) NMR SPECTROSCOPY
Overview
NMR spectroscopy has been used to study recombinant Escherichia coli CheY, a 128-residue protein involved in regulating bacterial chemotaxis. Heteronuclear three- and four-dimensional (3D and 4D) experiments have provided sequence-specific resonance assignments and quantitation of short-, medium-, and long-range distance restraints from nuclear Overhauser enhancement (NOE) intensities. These distance restraints were further supplemented with measurements of three-bond scalar coupling constants to define the local dihedral angles, and with the identification of amide protons undergoing slow solvent exchange from which hydrogen-bonding patterns were identified. The current model structure shows the same global fold of CheY as existing X-ray structures (Volz & Matsumura, 1991; Stock et al. 1993) with a (beta/alpha)5 motif of five parallel beta-strands at the central core surrounded by three alpha-helices on one face and with two on the opposite side. Heteronuclear 15N-1H relaxation experiments are interpreted to show portions of the protein structure in the Mg2+ binding loop are ill-defined because of slow motion (chemical exchange) on the NMR time scale. Moreover, the presence of Mg2+ disrupts the salt bridge between the highly conserved Lys-109 and Asp-57, the site of phosphorylation.
About this Structure
1CEY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy., Moy FJ, Lowry DF, Matsumura P, Dahlquist FW, Krywko JE, Domaille PJ, Biochemistry. 1994 Sep 6;33(35):10731-42. PMID:8075074
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