|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Erythrobacter litoralis EL346 blue-light activated histidine kinase== | | ==Erythrobacter litoralis EL346 blue-light activated histidine kinase== |
| - | <StructureSection load='4r3a' size='340' side='right' caption='[[4r3a]], [[Resolution|resolution]] 2.92Å' scene=''> | + | <StructureSection load='4r3a' size='340' side='right'caption='[[4r3a]], [[Resolution|resolution]] 2.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4r3a]] is a 2 chain structure. The March 2015 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Phototropin'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2015_3 10.2210/rcsb_pdb/mom_2015_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R3A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R3A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4r3a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Erythrobacter_litoralis_HTCC2594 Erythrobacter litoralis HTCC2594]. The March 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Phototropin'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_3 10.2210/rcsb_pdb/mom_2015_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R3A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</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]] 2.92Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r38|4r38]], [[4r39|4r39]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</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=4r3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3a OCA], [https://pdbe.org/4r3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r3a RCSB], [https://www.ebi.ac.uk/pdbsum/4r3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r3a ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3a OCA], [http://pdbe.org/4r3a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r3a RCSB], [http://www.ebi.ac.uk/pdbsum/4r3a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r3a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LVHK2_ERYLH LVHK2_ERYLH]] Photosensitive kinase that is involved in increased bacterial virulence upon exposure to light.<ref>PMID:17717187</ref> | + | [https://www.uniprot.org/uniprot/LVHK2_ERYLH LVHK2_ERYLH] Photosensitive kinase that is involved in increased bacterial virulence upon exposure to light.<ref>PMID:17717187</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Histidine kinase]] | + | [[Category: Erythrobacter litoralis HTCC2594]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Phototropin]] | | [[Category: Phototropin]] |
| | [[Category: RCSB PDB Molecule of the Month]] | | [[Category: RCSB PDB Molecule of the Month]] |
| - | [[Category: Gardner, K H]] | + | [[Category: Gardner KH]] |
| - | [[Category: Rivera-Cancel, G]] | + | [[Category: Rivera-Cancel G]] |
| - | [[Category: Tomchick, D R]] | + | [[Category: Tomchick DR]] |
| - | [[Category: Bergerat fold]]
| + | |
| - | [[Category: Cell signaling]]
| + | |
| - | [[Category: Light-activated]]
| + | |
| - | [[Category: Lov domain]]
| + | |
| - | [[Category: Photoreceptor]]
| + | |
| - | [[Category: Regulation]]
| + | |
| - | [[Category: Sensory transduction]]
| + | |
| - | [[Category: Signal transduction]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Two-component system]]
| + | |
| Structural highlights
Function
LVHK2_ERYLH Photosensitive kinase that is involved in increased bacterial virulence upon exposure to light.[1]
Publication Abstract from PubMed
Although histidine kinases (HKs) are critical sensors of external stimuli in prokaryotes, the mechanisms by which their sensor domains control enzymatic activity remain unclear. Here, we report the full-length structure of a blue light-activated HK from Erythrobacter litoralis HTCC2594 (EL346) and the results of biochemical and biophysical studies that explain how it is activated by light. Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer. Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain. The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark. Upon light stimulation, interdomain interactions weaken to facilitate activation. Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation. We suggest parallels between EL346 and dimeric HKs, with sensor-induced movements in the DHp similarly remodeling the DHp/CA interface as part of activation.
Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation.,Rivera-Cancel G, Ko WH, Tomchick DR, Correa F, Gardner KH Proc Natl Acad Sci U S A. 2014 Dec 16;111(50):17839-44. doi:, 10.1073/pnas.1413983111. Epub 2014 Dec 2. PMID:25468971[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Swartz TE, Tseng TS, Frederickson MA, Paris G, Comerci DJ, Rajashekara G, Kim JG, Mudgett MB, Splitter GA, Ugalde RA, Goldbaum FA, Briggs WR, Bogomolni RA. Blue-light-activated histidine kinases: two-component sensors in bacteria. Science. 2007 Aug 24;317(5841):1090-3. PMID:17717187 doi:http://dx.doi.org/10.1126/science.1144306
- ↑ Rivera-Cancel G, Ko WH, Tomchick DR, Correa F, Gardner KH. Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation. Proc Natl Acad Sci U S A. 2014 Dec 16;111(50):17839-44. doi:, 10.1073/pnas.1413983111. Epub 2014 Dec 2. PMID:25468971 doi:http://dx.doi.org/10.1073/pnas.1413983111
|
