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[[Image:1vb6.png|left|200px]]


{{STRUCTURE_1vb6|  PDB=1vb6  |  SCENE=  }}
==Crystal Structure of the heme PAS sensor domain of Ec DOS (oxygen-bound form)==
 
<StructureSection load='1vb6' size='340' side='right'caption='[[1vb6]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
===Crystal Structure of the heme PAS sensor domain of Ec DOS (oxygen-bound form)===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1vb6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VB6 FirstGlance]. <br>
{{ABSTRACT_PUBMED_018980385}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vb6 OCA], [https://pdbe.org/1vb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vb6 RCSB], [https://www.ebi.ac.uk/pdbsum/1vb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vb6 ProSAT]</span></td></tr>
[[1vb6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VB6 OCA].  
</table>
 
== Function ==
==Reference==
[https://www.uniprot.org/uniprot/DOSP_ECOLI DOSP_ECOLI] Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP (PubMed:15995192) but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate (PubMed:11970957). Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.<ref>PMID:20553324</ref>
<ref group="xtra">PMID:018980385</ref><references group="xtra"/>
== Evolutionary Conservation ==
[[Category: Escherichia coli k-12]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Kurokawa, H.]]
Check<jmol>
[[Category: Mikami, B.]]
  <jmolCheckbox>
[[Category: Sagami, I.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vb/1vb6_consurf.spt"</scriptWhenChecked>
[[Category: Shimizu, T.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
[[Category: Watanabe, M.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Heme]]
  </jmolCheckbox>
[[Category: Pa]]
</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=1vb6 ConSurf].
[[Category: Sensor]]
<div style="clear:both"></div>
[[Category: Signaling protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Kurokawa H]]
[[Category: Mikami B]]
[[Category: Sagami I]]
[[Category: Shimizu T]]
[[Category: Watanabe M]]