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| <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 with sequence from [http://en.wikipedia.org/wiki/"bacillus_thermodenitrificans"_klaushofer_and_hollaus_1970 "bacillus thermodenitrificans" klaushofer and hollaus 1970]. 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 [http://proteopedia.org/fgij/fg.htm?mol=5FQ1 FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></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'>[http://proteopedia.org/fgij/fg.htm?mol=5fq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fq1 OCA], [http://pdbe.org/5fq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fq1 RCSB], [http://www.ebi.ac.uk/pdbsum/5fq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fq1 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bacillus thermodenitrificans klaushofer and hollaus 1970]] | + | [[Category: Geobacillus thermodenitrificans]] |
- | [[Category: Histidine kinase]]
| + | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Becker, S]] | + | [[Category: Becker S]] |
- | [[Category: Giller, K]] | + | [[Category: Giller K]] |
- | [[Category: Schomburg, B]] | + | [[Category: Schomburg B]] |
- | [[Category: Cita]]
| + | |
- | [[Category: Pas domain]]
| + | |
- | [[Category: Transferase]]
| + | |
- | [[Category: Transmembrane signaling]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Weisenburger S, Boening D, Schomburg B, Giller K, Becker S, Griesinger C, Sandoghdar V. Cryogenic optical localization provides 3D protein structure data with Angstrom resolution. Nat Methods. 2017 Feb;14(2):141-144. doi: 10.1038/nmeth.4141. Epub 2017 Jan 9. PMID:28068317 doi:http://dx.doi.org/10.1038/nmeth.4141
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