1vb6
From Proteopedia
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| - | [[Image:1vb6.gif|left|200px]]<br /><applet load="1vb6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1vb6, resolution 1.56Å" /> | ||
| - | '''Crystal Structure of the heme PAS sensor domain of Ec DOS (oxygen-bound form)'''<br /> | ||
| - | == | + | ==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]] 1.56Å' scene=''> | |
| - | [[ | + | == 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> | |
| - | [ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56Å</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> |
| - | [ | + | <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> |
| - | [[ | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [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> |
| - | [[Category: | + | == Evolutionary Conservation == |
| - | [[Category: | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | [[Category: | + | Check<jmol> |
| - | [[Category: | + | <jmolCheckbox> |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vb/1vb6_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=1vb6 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == 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]] | ||
Current revision
Crystal Structure of the heme PAS sensor domain of Ec DOS (oxygen-bound form)
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