1nxp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nxp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1nxp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nxp| PDB=1nxp | SCENE= }}
{{STRUCTURE_1nxp| PDB=1nxp | SCENE= }}
-
'''MicArec pH4.5'''
+
===MicArec pH4.5===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15090529}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15090529 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15090529}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Riboldi-Tunnicliffe, A.]]
[[Category: Riboldi-Tunnicliffe, A.]]
[[Category: Doubly wound 5 alpha - 5 beta chain]]
[[Category: Doubly wound 5 alpha - 5 beta chain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:06:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:42:19 2008''

Revision as of 05:42, 28 July 2008

Image:1nxp.png

Template:STRUCTURE 1nxp

MicArec pH4.5

Template:ABSTRACT PUBMED 15090529

About this Structure

1NXP is a Single protein structure of sequence from Streptococcus pneumoniae tigr4. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jul 28 08:42:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nxp"
Personal tools