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1sr2

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Revision as of 08:01, 14 March 2018

Solution structure of the Escherichia coli YojN Histidine-Phosphotransferase (HPt) domain

Structural highlights

1sr2 is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	YOJN, B2216 ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RCSD_ECOLI] Component of the Rcs signaling system, which controls transcription of numerous genes. RcsD is a phosphotransfer intermediate between the sensor kinase RcsC and the response regulator RcsB. It acquires a phosphoryl group from RcsC and transfers it to RcsB. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.[HAMAP-Rule:MF_00980]^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Carballes F, Bertrand C, Bouche JP, Cam K. Regulation of Escherichia coli cell division genes ftsA and ftsZ by the two-component system rcsC-rcsB. Mol Microbiol. 1999 Nov;34(3):442-50. PMID:10564486
↑ Takeda S, Fujisawa Y, Matsubara M, Aiba H, Mizuno T. A novel feature of the multistep phosphorelay in Escherichia coli: a revised model of the RcsC --> YojN --> RcsB signalling pathway implicated in capsular synthesis and swarming behaviour. Mol Microbiol. 2001 Apr;40(2):440-50. PMID:11309126
↑ Chen MH, Takeda S, Yamada H, Ishii Y, Yamashino T, Mizuno T. Characterization of the RcsC-->YojN-->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli. Biosci Biotechnol Biochem. 2001 Oct;65(10):2364-7. PMID:11758943
↑ Hagiwara D, Sugiura M, Oshima T, Mori H, Aiba H, Yamashino T, Mizuno T. Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB phosphorelay system in Escherichia coli. J Bacteriol. 2003 Oct;185(19):5735-46. PMID:13129944
↑ Ferrieres L, Clarke DJ. The RcsC sensor kinase is required for normal biofilm formation in Escherichia coli K-12 and controls the expression of a regulon in response to growth on a solid surface. Mol Microbiol. 2003 Dec;50(5):1665-82. PMID:14651646
↑ Rogov VV, Bernhard F, Lohr F, Dotsch V. Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains. J Mol Biol. 2004 Oct 29;343(4):1035-48. PMID:15476819 doi:10.1016/j.jmb.2004.08.096

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sr2"

@@ Line 1: / Line 1: @@
 ==Solution structure of the Escherichia coli YojN Histidine-Phosphotransferase (HPt) domain==
 <StructureSection load='1sr2' size='340' side='right' caption='[[1sr2]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1sr2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SR2 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YOJN, B2216 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sr2 OCA], [http://pdbe.org/1sr2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sr2 RCSB], [http://www.ebi.ac.uk/pdbsum/1sr2 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sr2 OCA], [http://pdbe.org/1sr2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sr2 RCSB], [http://www.ebi.ac.uk/pdbsum/1sr2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sr2 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sr/1sr2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sr/1sr2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1sr2

From Proteopedia

Revision as of 08:01, 14 March 2018

Solution structure of the Escherichia coli YojN Histidine-Phosphotransferase (HPt) domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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