1sr2: Difference between revisions
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'''Solution structure of the Escherichia coli YojN Histidine-Phosphotransferase (HPt) domain''' | {{Structure | ||
|PDB= 1sr2 |SIZE=350|CAPTION= <scene name='initialview01'>1sr2</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= YOJN, B2216 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Solution structure of the Escherichia coli YojN Histidine-Phosphotransferase (HPt) domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SR2 is a [ | 1SR2 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=1SR2 OCA]. | ||
==Reference== | ==Reference== | ||
Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains., Rogov VV, Bernhard F, Lohr F, Dotsch V, J Mol Biol. 2004 Oct 29;343(4):1035-48. PMID:[http:// | Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains., Rogov VV, Bernhard F, Lohr F, Dotsch V, J Mol Biol. 2004 Oct 29;343(4):1035-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15476819 15476819] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: four-helical bundle]] | [[Category: four-helical bundle]] | ||
''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 14:08:38 2008'' | ||
Revision as of 15:08, 20 March 2008
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| Gene: | YOJN, B2216 (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the Escherichia coli YojN Histidine-Phosphotransferase (HPt) domain
OverviewOverview
The Rcs signaling system in Escherichia coli controls a variety of physiological functions, including capsule synthesis, cell division and motility. The activity of the central regulator RcsB is modulated by phosphorylation through the sensor kinases YojN and RcsC, with the YojN histidine phosphotransferase (HPt) domain representing the catalytic unit that coordinates the potentially reversible phosphotransfer reaction between the receiver domains of the RcsB and RcsC proteins. Heteronuclear high-resolution NMR spectroscopy was employed to determine the solution structure of the YojN-HPt domain and to map the interaction with its two cognate receiver domains. The solution structure of YojN-HPt exhibits a well-ordered and rigid protein core consisting of the five helices alphaI to alphaV. The helices alphaII to alphaV form a four-helix bundle signature motif common to proteins of similar function, and helix alphaI forms a cap on top of the bundle. The helix alphaII is separated by a proline induced kink into two parts with different orientations and dynamic behavior that is potentially important for complex formation with other proteins. The N-terminal part of YojN-HPt spanning the first 26 amino acid residues seems to contain neither a regular secondary structure nor a stable tertiary structure and is disordered in solution. The identified YojN-HPt recognition sites for the regulator RcsB and for the isolated receiver domain of the RcsC kinase largely overlap in defined regions of the helices alphaII and alphaIII, but show significant differences. Using the residues with the largest chemical shift changes obtained from titration experiments, we observed a dissociation constant of approximately 200microM for YojN-HPt/RcsC-PR and of 40microM for YojN-HPt/RcsB complexes. Our data indicate the presence of a recognition area in close vicinity to the active-site histidine residue of HPt domains as a determinant of specificity in signal-transduction pathways.
About this StructureAbout this Structure
1SR2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains., Rogov VV, Bernhard F, Lohr F, Dotsch V, J Mol Biol. 2004 Oct 29;343(4):1035-48. PMID:15476819
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