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[[Image:1mvo.jpg|left|200px]]


{{Structure
==Crystal structure of the PhoP receiver domain from Bacillus subtilis==
|PDB= 1mvo |SIZE=350|CAPTION= <scene name='initialview01'>1mvo</scene>, resolution 1.6&Aring;
<StructureSection load='1mvo' size='340' side='right'caption='[[1mvo]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
<table><tr><td colspan='2'>[[1mvo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MVO FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
|GENE= PHOP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1mvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvo OCA], [https://pdbe.org/1mvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mvo RCSB], [https://www.ebi.ac.uk/pdbsum/1mvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHOP_BACSU PHOP_BACSU] Member of the two-component regulatory system PhoP/PhoR involved in the regulation of alkaline phosphatase genes phoA and phoB and of phosphodiesterase.
== 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/mv/1mvo_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=1mvo ConSurf].
<div style="clear:both"></div>


'''Crystal structure of the PhoP receiver domain from Bacillus subtilis'''
==See Also==
 
*[[PhoP-PhoQ|PhoP-PhoQ]]
 
*[[Response regulator 3D structure|Response regulator 3D structure]]
==Overview==
__TOC__
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.
</StructureSection>
 
==About this Structure==
1MVO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVO 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:[http://www.ncbi.nlm.nih.gov/pubmed/12486062 12486062]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Birck, C.]]
[[Category: Birck C]]
[[Category: Chen, Y.]]
[[Category: Chen Y]]
[[Category: Hulett, F M.]]
[[Category: Hulett FM]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: Samama JP]]
[[Category: Samama, J P.]]
[[Category: MN]]
[[Category: NA]]
[[Category: alpha/beta doubly wound fold]]
[[Category: asymmetric interface]]
[[Category: phosphate regulon]]
[[Category: phosphorylation]]
[[Category: response regulator]]
[[Category: spine]]
[[Category: structural genomic]]
[[Category: structural proteomics in europe]]
[[Category: tandem association]]
[[Category: transcriptional regulatory protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:48:46 2008''

Latest revision as of 13:27, 13 March 2024

Crystal structure of the PhoP receiver domain from Bacillus subtilis

1mvo, resolution 1.60Å

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