1mvo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mvo.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1mvo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mvo| PDB=1mvo | SCENE= }}
{{STRUCTURE_1mvo| PDB=1mvo | SCENE= }}
-
'''Crystal structure of the PhoP receiver domain from Bacillus subtilis'''
+
===Crystal structure of the PhoP receiver domain from Bacillus subtilis===
-
==Overview==
+
<!--
-
PhoP from Bacillus subtilis belongs to the OmpR subfamily of response regulators. It regulates the transcription of several operons and participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency. The receiver domains of two members of this subfamily, PhoB from Escherichia coli and DrrD from Thermotoga maritima, have been structurally characterized. These modules have similar overall folds but display remarkable differences in the conformation of the beta4-alpha4 and alpha4 regions. The crystal structure of the receiver domain of PhoP (PhoPN) described in this paper illustrates yet another geometry in this region. Another major issue of the structure determination is the dimeric state of the protein and the novel mode of association between receiver domains. The protein-protein interface is provided by two different surfaces from each protomer, and the tandem unit formed through this asymmetric interface leaves free interaction surfaces. This design is well suited for further association of PhoP dimers to form oligomeric structures. The interprotein interface buries 970 A(2) from solvent and mostly involves interactions between charged residues. As described in the accompanying paper, mutations of a single residue in one salt bridge shielded from solvent prevented dimerization of the unphosphorylated and phosphorylated response regulator and had drastic functional consequences. The three structurally documented members of the OmpR family (PhoB, DrrD, and PhoP) provide a framework to consider possible relationships between structural features and sequence signatures in critical regions of the receiver domains.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12486062}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12486062 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12486062}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Tandem association]]
[[Category: Tandem association]]
[[Category: Transcriptional regulatory protein]]
[[Category: Transcriptional regulatory protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:07:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:07:10 2008''

Revision as of 10:07, 27 July 2008

Image:1mvo.png

Template:STRUCTURE 1mvo

Crystal structure of the PhoP receiver domain from Bacillus subtilis

Template:ABSTRACT PUBMED 12486062

About this Structure

1MVO is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface., Birck C, Chen Y, Hulett FM, Samama JP, J Bacteriol. 2003 Jan;185(1):254-61. PMID:12486062

Page seeded by OCA on Sun Jul 27 13:07:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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