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5fq1
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==Structure of the cytoplasmic PAS domain of the Geobacillus thermodenitrificans histidine kinase CitA== | ==Structure of the cytoplasmic PAS domain of the Geobacillus thermodenitrificans histidine kinase CitA== | ||
| - | <StructureSection load='5fq1' size='340' side='right' caption='[[5fq1]], [[Resolution|resolution]] 1.76Å' scene=''> | + | <StructureSection load='5fq1' size='340' side='right'caption='[[5fq1]], [[Resolution|resolution]] 1.76Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5fq1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FQ1 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5fq1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans Geobacillus thermodenitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FQ1 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5fq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fq1 OCA], [https://pdbe.org/5fq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fq1 RCSB], [https://www.ebi.ac.uk/pdbsum/5fq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fq1 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A4IPE6_GEOTN A4IPE6_GEOTN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We introduce Cryogenic Optical Localization in 3D (COLD), a method to localize multiple fluorescent sites within a single small protein with Angstrom resolution. We demonstrate COLD by determining the conformational state of the cytosolic Per-ARNT-Sim domain from the histidine kinase CitA of Geobacillus thermodenitrificans and resolving the four biotin sites of streptavidin. COLD provides quantitative 3D information about small- to medium-sized biomolecules on the Angstrom scale and complements other techniques in structural biology. | ||
| + | |||
| + | Cryogenic optical localization provides 3D protein structure data with Angstrom resolution.,Weisenburger S, Boening D, Schomburg B, Giller K, Becker S, Griesinger C, Sandoghdar V Nat Methods. 2017 Feb;14(2):141-144. doi: 10.1038/nmeth.4141. Epub 2017 Jan 9. PMID:28068317<ref>PMID:28068317</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5fq1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Geobacillus thermodenitrificans]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Becker S]] |
| - | [[Category: | + | [[Category: Giller K]] |
| - | [[Category: | + | [[Category: Schomburg B]] |
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| - | + | ||
| - | + | ||
Current revision
Structure of the cytoplasmic PAS domain of the Geobacillus thermodenitrificans histidine kinase CitA
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