1v9z

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{{Seed}}
 
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[[Image:1v9z.png|left|200px]]
 
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==Crystal Structure of the heme PAS sensor domain of Ec DOS (Ferrous Form)==
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The line below this paragraph, containing "STRUCTURE_1v9z", creates the "Structure Box" on the page.
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<StructureSection load='1v9z' size='340' side='right'caption='[[1v9z]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1v9z]] 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=1V9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V9Z FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<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></td></tr>
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{{STRUCTURE_1v9z| PDB=1v9z | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9z OCA], [https://pdbe.org/1v9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v9z RCSB], [https://www.ebi.ac.uk/pdbsum/1v9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v9z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v9/1v9z_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1v9z ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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PAS domains, which have been identified in over 1100 proteins from all three kingdoms of life, convert various input stimuli into signals that propagate to downstream components by modifying protein-protein interactions. One such protein is the Escherichia coli redox sensor, Ec DOS, a phosphodiesterase that degrades cyclic adenosine monophosphate in a redox-dependent manner. Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively. The protein folds into a characteristic PAS domain structure and forms a homodimer. In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule. Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other. The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
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===Crystal Structure of the heme PAS sensor domain of Ec DOS (Ferrous Form)===
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A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor.,Kurokawa H, Lee DS, Watanabe M, Sagami I, Mikami B, Raman CS, Shimizu T J Biol Chem. 2004 May 7;279(19):20186-93. Epub 2004 Feb 23. PMID:14982921<ref>PMID:14982921</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_14982921}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1v9z" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14982921 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14982921}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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1V9Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9Z OCA].
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[[Category: Large Structures]]
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[[Category: Kurokawa H]]
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==Reference==
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[[Category: Lee DS]]
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A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor., Kurokawa H, Lee DS, Watanabe M, Sagami I, Mikami B, Raman CS, Shimizu T, J Biol Chem. 2004 May 7;279(19):20186-93. Epub 2004 Feb 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14982921 14982921]
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[[Category: Mikami B]]
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[[Category: Escherichia coli]]
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[[Category: Raman CS]]
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[[Category: Single protein]]
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[[Category: Sagami I]]
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[[Category: Kurokawa, H.]]
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[[Category: Shimizu T]]
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[[Category: Lee, D S.]]
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[[Category: Watanabe M]]
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[[Category: Mikami, B.]]
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[[Category: Raman, C S.]]
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[[Category: Sagami, I.]]
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[[Category: Shimizu, T.]]
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[[Category: Watanabe, M.]]
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[[Category: Heme]]
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[[Category: Pa]]
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[[Category: Sensor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:57:21 2008''
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Current revision

Crystal Structure of the heme PAS sensor domain of Ec DOS (Ferrous Form)

PDB ID 1v9z

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