1ntr

From Proteopedia

(Difference between revisions)

Current revision

SOLUTION STRUCTURE OF THE N-TERMINAL RECEIVER DOMAIN OF NTRC

Structural highlights

1ntr is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NTRC_SALTY Member of the two-component regulatory system NtrB/NtrC involved in the activation of nitrogen assimilatory genes such as GlnA. NtrC is phosphorylated by NtrB and interacts with sigma-54.

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

NTRC is a transcriptional enhancer binding protein whose N-terminal domain is a member of the family of receiver domains of two-component regulatory systems. Using 3D and 4D NMR spectroscopy, we have completed the 1H, 15N, and 13C assignments and determined the solution structure of the N-terminal receiver domain of the NTRC protein. Determination of the three-dimensional structure was carried out with the program X-PLOR (Brunger, 1992) using a total of 915 NMR-derived distance and dihedral angle restraints. The resultant family of structures has an average root mean square deviation of 0.81 A from the average structure for the backbone atoms involved in well-defined secondary structure. The structure is comprised of five alpha-helices and a five-stranded parallel beta-sheet, in a (beta/alpha)5 topology. Comparison of the solution structure of the NTRC receiver domain with the crystal structures of the homologous protein CheY in both the Mg(2+)-free and Mg(2+)-bound forms [Stock, A.M., Mottonen, J. M., Stock, J. B., & Schutt, C. E. (1989) Nature 337, 745-749; Volz, K., & Matsumura, P. (1991) J. Biol. Chem. 296, 15511-15519; Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., & Petsko, G. A. (1993) Biochemistry 32, 13375-13380; Bellsolell, L., Prieto, J., Serrano, L., & Coll, M. (1994) J. Mol. Biol. 238, 489-495] reveals a very similar fold, with the only significant difference occurring in the positioning of helix 4 relative to the rest of the protein. Examination of the conformation of consensus residues of the receiver domain superfamily [Volz, K. (1993) Biochemistry 32, 11741-11753] in the structures of the NTRC receiver domain and CheY establishes the structural importance of residues whose side chains are involved in hydrogen bonding or hydrophobic core interactions. The importance of some nonconsensus residues which may be conserved for their ability to fulfill helix capping roles is also discussed.

Three-dimensional solution structure of the N-terminal receiver domain of NTRC.,Volkman BF, Nohaile MJ, Amy NK, Kustu S, Wemmer DE Biochemistry. 1995 Jan 31;34(4):1413-24. PMID:7827089^[1]

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

References

↑ Volkman BF, Nohaile MJ, Amy NK, Kustu S, Wemmer DE. Three-dimensional solution structure of the N-terminal receiver domain of NTRC. Biochemistry. 1995 Jan 31;34(4):1413-24. PMID:7827089

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/1ntr"

@@ Line 1: / Line 1: @@
-[[Image:1ntr.jpg|left|200px]]<br /><applet load="1ntr" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ntr" />
-'''SOLUTION STRUCTURE OF THE N-TERMINAL RECEIVER DOMAIN OF NTRC'''<br />
-==Overview==
+==SOLUTION STRUCTURE OF THE N-TERMINAL RECEIVER DOMAIN OF NTRC==
-NTRC is a transcriptional enhancer binding protein whose N-terminal domain, is a member of the family of receiver domains of two-component regulatory, systems. Using 3D and 4D NMR spectroscopy, we have completed the 1H, 15N, and 13C assignments and determined the solution structure of the, N-terminal receiver domain of the NTRC protein. Determination of the, three-dimensional structure was carried out with the program X-PLOR, (Brunger, 1992) using a total of 915 NMR-derived distance and dihedral, angle restraints. The resultant family of structures has an average root, mean square deviation of 0.81 A from the average structure for the, backbone atoms involved in well-defined secondary structure. The structure, is comprised of five alpha-helices and a five-stranded parallel, beta-sheet, in a (beta/alpha)5 topology. Comparison of the solution, structure of the NTRC receiver domain with the crystal structures of the, homologous protein CheY in both the Mg(2+)-free and Mg(2+)-bound forms, [Stock, A.M., Mottonen, J. M., Stock, J. B., &amp; Schutt, C. E. (1989) Nature, 337, 745-749; Volz, K., &amp; Matsumura, P. (1991) J. Biol. Chem. 296, 15511-15519; Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., &amp; Petsko, G. A. (1993) Biochemistry 32, 13375-13380; Bellsolell, L., Prieto, J., Serrano, L., &amp; Coll, M. (1994) J., Mol. Biol. 238, 489-495] reveals a very similar fold, with the only, significant difference occurring in the positioning of helix 4 relative to, the rest of the protein. Examination of the conformation of consensus, residues of the receiver domain superfamily [Volz, K. (1993) Biochemistry, 32, 11741-11753] in the structures of the NTRC receiver domain and CheY, establishes the structural importance of residues whose side chains are, involved in hydrogen bonding or hydrophobic core interactions. The, importance of some nonconsensus residues which may be conserved for their, ability to fulfill helix capping roles is also discussed.
+<StructureSection load='1ntr' size='340' side='right'caption='[[1ntr]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ntr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NTR FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ntr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ntr OCA], [https://pdbe.org/1ntr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ntr RCSB], [https://www.ebi.ac.uk/pdbsum/1ntr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ntr ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NTRC_SALTY NTRC_SALTY] Member of the two-component regulatory system NtrB/NtrC involved in the activation of nitrogen assimilatory genes such as GlnA. NtrC is phosphorylated by NtrB and interacts with sigma-54.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nt/1ntr_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ntr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+NTRC is a transcriptional enhancer binding protein whose N-terminal domain is a member of the family of receiver domains of two-component regulatory systems. Using 3D and 4D NMR spectroscopy, we have completed the 1H, 15N, and 13C assignments and determined the solution structure of the N-terminal receiver domain of the NTRC protein. Determination of the three-dimensional structure was carried out with the program X-PLOR (Brunger, 1992) using a total of 915 NMR-derived distance and dihedral angle restraints. The resultant family of structures has an average root mean square deviation of 0.81 A from the average structure for the backbone atoms involved in well-defined secondary structure. The structure is comprised of five alpha-helices and a five-stranded parallel beta-sheet, in a (beta/alpha)5 topology. Comparison of the solution structure of the NTRC receiver domain with the crystal structures of the homologous protein CheY in both the Mg(2+)-free and Mg(2+)-bound forms [Stock, A.M., Mottonen, J. M., Stock, J. B., &amp; Schutt, C. E. (1989) Nature 337, 745-749; Volz, K., &amp; Matsumura, P. (1991) J. Biol. Chem. 296, 15511-15519; Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., &amp; Petsko, G. A. (1993) Biochemistry 32, 13375-13380; Bellsolell, L., Prieto, J., Serrano, L., &amp; Coll, M. (1994) J. Mol. Biol. 238, 489-495] reveals a very similar fold, with the only significant difference occurring in the positioning of helix 4 relative to the rest of the protein. Examination of the conformation of consensus residues of the receiver domain superfamily [Volz, K. (1993) Biochemistry 32, 11741-11753] in the structures of the NTRC receiver domain and CheY establishes the structural importance of residues whose side chains are involved in hydrogen bonding or hydrophobic core interactions. The importance of some nonconsensus residues which may be conserved for their ability to fulfill helix capping roles is also discussed.
-==About this Structure==
+Three-dimensional solution structure of the N-terminal receiver domain of NTRC.,Volkman BF, Nohaile MJ, Amy NK, Kustu S, Wemmer DE Biochemistry. 1995 Jan 31;34(4):1413-24. PMID:7827089<ref>PMID:7827089</ref>
-NTR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NTR OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Three-dimensional solution structure of the N-terminal receiver domain of NTRC., Volkman BF, Nohaile MJ, Amy NK, Kustu S, Wemmer DE, Biochemistry. 1995 Jan 31;34(4):1413-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7827089 7827089]
+</div>
-[[Category: Salmonella typhimurium]]
+<div class="pdbe-citations 1ntr" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+== References ==
-[[Category: Amy, N.K.]]
+<references/>
-[[Category: Kustu, S.]]
+__TOC__
-[[Category: Nohaile, M.J.]]
+</StructureSection>
-[[Category: Volkman, B.F.]]
+[[Category: Large Structures]]
-[[Category: Wemmer, D.E.]]
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-[[Category: receiver domain]]
+[[Category: Amy NK]]
-[[Category: two-component system]]
+[[Category: Kustu S]]
+[[Category: Nohaile MJ]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:33:01 2007''
+[[Category: Volkman BF]]
+[[Category: Wemmer DE]]

1ntr

From Proteopedia

Current revision

SOLUTION STRUCTURE OF THE N-TERMINAL RECEIVER DOMAIN OF NTRC

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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