1nxp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1nxp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nxp, resolution 1.82&Aring;" /> '''MicArec pH4.5'''<br ...)
Current revision (09:26, 16 August 2023) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1nxp.gif|left|200px]]<br /><applet load="1nxp" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1nxp, resolution 1.82&Aring;" />
 
-
'''MicArec pH4.5'''<br />
 
-
==Overview==
+
==MicArec pH4.5==
-
A variety of bacterial cellular responses to environmental signals are, mediated by two-component signal transduction systems comprising a, membrane-associated histidine protein kinase and a cytoplasmic response, regulator (RR), which interpret specific stimuli and produce a measured, physiological response. In RR activation, transient phosphorylation of a, highly conserved aspartic acid residue drives the conformation changes, needed for full activation of the protein. Sequence homology reveals that, RR02 from Streptococcus pneumoniae belongs to the OmpR subfamily of RRs., The structures of the receiver domains from four members of this family, DrrB and DrrD from Thermotoga maritima, PhoB from Escherichia coli, and, PhoP from Bacillus subtilis, have been elucidated. These domains are, globally very similar in that they are composed of a doubly wound, alpha(5)beta(5); however, they differ remarkably in the fine detail of the, beta4-alpha4 and alpha4 regions. The structures presented here reveal a, further difference of the geometry in this region. RR02 is has been shown, to be the essential RR in the gram-positive bacterium S. pneumoniae R., Lange, C. Wagner, A. de Saizieu, N. Flint, J. Molnos, M. Stieger, P., Caspers, M. Kamber, W. Keck, and K. E. Amrein, Gene 237:223-234, 1999; J., P. Throup, K. K. Koretke, A. P. Bryant, K. A. Ingraham, A. F. Chalker, Y., Ge, A. Marra, N. G. Wallis, J. R. Brown, D. J. Holmes, M. Rosenberg, and, M. K. Burnham, Mol. Microbiol. 35:566-576, 2000). RR02 functions as part, of a phosphotransfer system that ultimately controls the levels of, competence within the bacteria. Here we report the native structure of the, receiver domain of RR02 from serotype 4 S. pneumoniae (as well as acetate-, and phosphate-bound forms) at different pH levels. Two native structures, at 2.3 A, phased by single-wavelength anomalous diffraction (xenon SAD), and 1.85 A and a third structure at pH 5.9 revealed the presence of a, phosphate ion outside the active site. The fourth structure revealed the, presence of an acetate molecule in the active site.
+
<StructureSection load='1nxp' size='340' side='right'caption='[[1nxp]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1nxp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NXP FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene></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=1nxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nxp OCA], [https://pdbe.org/1nxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nxp RCSB], [https://www.ebi.ac.uk/pdbsum/1nxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nxp ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q9S1K0_STREE Q9S1K0_STREE]
 +
== 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/nx/1nxp_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=1nxp ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
A variety of bacterial cellular responses to environmental signals are mediated by two-component signal transduction systems comprising a membrane-associated histidine protein kinase and a cytoplasmic response regulator (RR), which interpret specific stimuli and produce a measured physiological response. In RR activation, transient phosphorylation of a highly conserved aspartic acid residue drives the conformation changes needed for full activation of the protein. Sequence homology reveals that RR02 from Streptococcus pneumoniae belongs to the OmpR subfamily of RRs. The structures of the receiver domains from four members of this family, DrrB and DrrD from Thermotoga maritima, PhoB from Escherichia coli, and PhoP from Bacillus subtilis, have been elucidated. These domains are globally very similar in that they are composed of a doubly wound alpha(5)beta(5); however, they differ remarkably in the fine detail of the beta4-alpha4 and alpha4 regions. The structures presented here reveal a further difference of the geometry in this region. RR02 is has been shown to be the essential RR in the gram-positive bacterium S. pneumoniae R. Lange, C. Wagner, A. de Saizieu, N. Flint, J. Molnos, M. Stieger, P. Caspers, M. Kamber, W. Keck, and K. E. Amrein, Gene 237:223-234, 1999; J. P. Throup, K. K. Koretke, A. P. Bryant, K. A. Ingraham, A. F. Chalker, Y. Ge, A. Marra, N. G. Wallis, J. R. Brown, D. J. Holmes, M. Rosenberg, and M. K. Burnham, Mol. Microbiol. 35:566-576, 2000). RR02 functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. Here we report the native structure of the receiver domain of RR02 from serotype 4 S. pneumoniae (as well as acetate- and phosphate-bound forms) at different pH levels. Two native structures at 2.3 A, phased by single-wavelength anomalous diffraction (xenon SAD), and 1.85 A and a third structure at pH 5.9 revealed the presence of a phosphate ion outside the active site. The fourth structure revealed the presence of an acetate molecule in the active site.
-
==About this Structure==
+
Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states.,Bent CJ, Isaacs NW, Mitchell TJ, Riboldi-Tunnicliffe A J Bacteriol. 2004 May;186(9):2872-9. PMID:15090529<ref>PMID:15090529</ref>
-
1NXP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae_tigr4 Streptococcus pneumoniae tigr4] with PHS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NXP OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states., Bent CJ, Isaacs NW, Mitchell TJ, Riboldi-Tunnicliffe A, J Bacteriol. 2004 May;186(9):2872-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15090529 15090529]
+
</div>
-
[[Category: Single protein]]
+
<div class="pdbe-citations 1nxp" style="background-color:#fffaf0;"></div>
-
[[Category: Streptococcus pneumoniae tigr4]]
+
-
[[Category: Bent, C.J.]]
+
-
[[Category: Isaacs, N.W.]]
+
-
[[Category: Mitchell, T.J.]]
+
-
[[Category: Riboldi-Tunnicliffe, A.]]
+
-
[[Category: PHS]]
+
-
[[Category: doubly wound 5 alpha - 5 beta chain]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:59:28 2007''
+
==See Also==
 +
*[[Response regulator 3D structure|Response regulator 3D structure]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Streptococcus pneumoniae TIGR4]]
 +
[[Category: Bent CJ]]
 +
[[Category: Isaacs NW]]
 +
[[Category: Mitchell TJ]]
 +
[[Category: Riboldi-Tunnicliffe A]]

Current revision

MicArec pH4.5

PDB ID 1nxp

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools