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[[Image:2fxa.gif|left|200px]]


{{Structure
==Structure of the Protease Production Regulatory Protein hpr from Bacillus subtilis.==
|PDB= 2fxa |SIZE=350|CAPTION= <scene name='initialview01'>2fxa</scene>, resolution 2.40&Aring;
<StructureSection load='2fxa' size='340' side='right'caption='[[2fxa]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene> and <scene name='pdbligand=1PE:PENTAETHYLENE GLYCOL'>1PE</scene>
<table><tr><td colspan='2'>[[2fxa]] is a 4 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=2FXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FXA 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]] 2.4&#8491;</td></tr>
|GENE= hpr, catA, scoC ([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=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=2fxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fxa OCA], [https://pdbe.org/2fxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fxa RCSB], [https://www.ebi.ac.uk/pdbsum/2fxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fxa ProSAT], [https://www.topsan.org/Proteins/MCSG/2fxa TOPSAN]</span></td></tr>
 
</table>
'''Structure of the Protease Production Regulatory Protein hpr from Bacillus subtilis.'''
== Function ==
 
[https://www.uniprot.org/uniprot/HPR_BACSU HPR_BACSU] Negative regulator of protease production and sporulation. Acts by binding directly to the promoter of protease genes (aprE and nprE), and by repressing oligopeptide permease operons (appABCDF and oppABCDF), thereby preventing uptake of oligopeptides required for initiation of sporulation. Acts with SinR as a corepressor of epr expression.<ref>PMID:1906467</ref> <ref>PMID:10383984</ref> <ref>PMID:16923912</ref>
 
== Evolutionary Conservation ==
==About this Structure==
[[Image:Consurf_key_small.gif|200px|right]]
2FXA 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=2FXA OCA].  
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fx/2fxa_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2fxa ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cuff, M E.]]
[[Category: Cuff ME]]
[[Category: Edwards, A.]]
[[Category: Edwards A]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak A]]
[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: Savchenko A]]
[[Category: Savchenko, A.]]
[[Category: Skarina T]]
[[Category: Skarina, T.]]
[[Category: 1PE]]
[[Category: EDO]]
[[Category: P6G]]
[[Category: PGE]]
[[Category: bacillus subtili]]
[[Category: hpr]]
[[Category: mcsg]]
[[Category: midwest center for structural genomic]]
[[Category: protease porduction]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: regulation]]
[[Category: structural genomic]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:57:52 2008''

Latest revision as of 12:07, 6 November 2024

Structure of the Protease Production Regulatory Protein hpr from Bacillus subtilis.Structure of the Protease Production Regulatory Protein hpr from Bacillus subtilis.

Structural highlights

2fxa is a 4 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

HPR_BACSU Negative regulator of protease production and sporulation. Acts by binding directly to the promoter of protease genes (aprE and nprE), and by repressing oligopeptide permease operons (appABCDF and oppABCDF), thereby preventing uptake of oligopeptides required for initiation of sporulation. Acts with SinR as a corepressor of epr expression.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Kallio PT, Fagelson JE, Hoch JA, Strauch MA. The transition state regulator Hpr of Bacillus subtilis is a DNA-binding protein. J Biol Chem. 1991 Jul 15;266(20):13411-7. PMID:1906467
  2. ↑ Koide A, Perego M, Hoch JA. ScoC regulates peptide transport and sporulation initiation in Bacillus subtilis. J Bacteriol. 1999 Jul;181(13):4114-7. PMID:10383984
  3. ↑ Kodgire P, Dixit M, Rao KK. ScoC and SinR negatively regulate epr by corepression in Bacillus subtilis. J Bacteriol. 2006 Sep;188(17):6425-8. PMID:16923912 doi:10.1128/JB.00427-06

2fxa, resolution 2.40Å

Drag the structure with the mouse to rotate

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