1s67

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(New page: 200px<br /><applet load="1s67" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s67, resolution 1.5&Aring;" /> '''Crystal structure of ...)
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[[Image:1s67.jpg|left|200px]]<br /><applet load="1s67" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1s67, resolution 1.5&Aring;" />
 
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'''Crystal structure of heme domain of direct oxygen sensor from E. coli'''<br />
 
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==Overview==
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==Crystal structure of heme domain of direct oxygen sensor from E. coli==
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The X-ray crystal structure of the Escherichia coli (Ec) direct oxygen, sensor heme domain (Ec DosH) has been solved to 1.8 A using Fe, multiple-wavelength anomalous dispersion (MAD), and the positions of Met95, have been confirmed by selenomethionine ((Se)Met) MAD. Ec DosH is the, sensing part of a larger two-domain sensing/signaling protein, in which, the signaling domain has phosphodiesterase activity. The asymmetric unit, of the crystal lattice contains a dimer comprised of two differently, ligated heme domain monomers. Except for the heme ligands, the monomer, heme domains are identical. In one monomer, the heme is ligated by, molecular oxygen (O(2)), while in the other monomer, an endogenous Met95, with S --&gt; Fe ligation replaces the exogenous O(2) ligand. In both heme, domains, the proximal ligand is His77. Analysis of these structures, reveals sizable ligand-dependent conformational changes in the protein, chain localized in the FG turn, the G(beta)-strand, and the HI turn. These, changes provide insight to the mechanism of signal propagation within the, heme domain following initiation due to O(2) dissociation.
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<StructureSection load='1s67' size='340' side='right'caption='[[1s67]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1s67]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S67 FirstGlance]. <br>
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1S67 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with HEM and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S67 OCA].
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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]] 1.5&#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>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
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==Reference==
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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=1s67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s67 OCA], [https://pdbe.org/1s67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s67 RCSB], [https://www.ebi.ac.uk/pdbsum/1s67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s67 ProSAT]</span></td></tr>
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Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH)., Park H, Suquet C, Satterlee JD, Kang C, Biochemistry. 2004 Mar 16;43(10):2738-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15005609 15005609]
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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/s6/1s67_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=1s67 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kang, C.H.]]
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[[Category: Kang CH]]
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[[Category: Park, H.J.]]
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[[Category: Park HJ]]
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[[Category: Satterlee, J.D.]]
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[[Category: Satterlee JD]]
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[[Category: Suquet, C.]]
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[[Category: Suquet C]]
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[[Category: HEM]]
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[[Category: OXY]]
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[[Category: e.coli]]
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[[Category: heme]]
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[[Category: oxygen storage/transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:08:47 2007''
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Current revision

Crystal structure of heme domain of direct oxygen sensor from E. coli

PDB ID 1s67

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