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3ehg
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3ehg is ON HOLD Authors: Trajtenberg, F., Buschiazzo, A. Description: Crystal structure of the ATP-binding domain of DesK in complex with ATP ''Pa...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the ATP-binding domain of DesK in complex with ATP== | |
| - | + | <StructureSection load='3ehg' size='340' side='right'caption='[[3ehg]], [[Resolution|resolution]] 1.74Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3ehg]] is a 1 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=3EHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EHG 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]] 1.74Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3ehg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ehg OCA], [https://pdbe.org/3ehg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ehg RCSB], [https://www.ebi.ac.uk/pdbsum/3ehg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ehg ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DESK_BACSU DESK_BACSU] Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase. Acts as a sensor of the membrane fluidity. Probably activates DesR by phosphorylation.<ref>PMID:11285232</ref> <ref>PMID:11717295</ref> <ref>PMID:12207704</ref> <ref>PMID:14734164</ref> <ref>PMID:15090506</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eh/3ehg_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=3ehg ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus subtilis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Buschiazzo A]] | ||
| + | [[Category: Trajtenberg F]] | ||
Current revision
Crystal structure of the ATP-binding domain of DesK in complex with ATP
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