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| | ==Light-induced intermediate structure L3 of P. aeruginosa bacteriophytochrome== | | ==Light-induced intermediate structure L3 of P. aeruginosa bacteriophytochrome== |
| - | <StructureSection load='3nou' size='340' side='right' caption='[[3nou]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='3nou' size='340' side='right'caption='[[3nou]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nou]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NOU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NOU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nou]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NOU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</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]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nhq|3nhq]], [[3nop|3nop]], [[3not|3not]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bphP, PA4117 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=3nou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nou OCA], [https://pdbe.org/3nou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nou RCSB], [https://www.ebi.ac.uk/pdbsum/3nou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nou ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nou OCA], [http://pdbe.org/3nou PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nou RCSB], [http://www.ebi.ac.uk/pdbsum/3nou PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nou ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BPHY_PSEAE BPHY_PSEAE]] Photoreceptor which exists in two forms that are reversibly interconvertible by light: the R form that absorbs maximally in the red region of the spectrum and the FR form that absorbs maximally in the far-red region (By similarity). | + | [https://www.uniprot.org/uniprot/BPHY_PSEAE BPHY_PSEAE] Photoreceptor which exists in two forms that are reversibly interconvertible by light: the R form that absorbs maximally in the red region of the spectrum and the FR form that absorbs maximally in the far-red region (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Histidine kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Moffat, K]] | + | [[Category: Moffat K]] |
| - | [[Category: Ren, Z]] | + | [[Category: Ren Z]] |
| - | [[Category: Yang, X]] | + | [[Category: Yang X]] |
| - | [[Category: Intermediate structure]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
BPHY_PSEAE Photoreceptor which exists in two forms that are reversibly interconvertible by light: the R form that absorbs maximally in the red region of the spectrum and the FR form that absorbs maximally in the far-red region (By similarity).
Publication Abstract from PubMed
Light is a fundamental signal that regulates important physiological processes such as development and circadian rhythm in living organisms. Phytochromes form a major family of photoreceptors responsible for red light perception in plants, fungi and bacteria. They undergo reversible photoconversion between red-absorbing (Pr) and far-red-absorbing (Pfr) states, thereby ultimately converting a light signal into a distinct biological signal that mediates subsequent cellular responses. Several structures of microbial phytochromes have been determined in their dark-adapted Pr or Pfr states. However, the structural nature of initial photochemical events has not been characterized by crystallography. Here we report the crystal structures of three intermediates in the photoreaction of Pseudomonas aeruginosa bacteriophytochrome (PaBphP). We used cryotrapping crystallography to capture intermediates, and followed structural changes by scanning the temperature at which the photoreaction proceeded. Light-induced conformational changes in PaBphP originate in ring D of the biliverdin (BV) chromophore, and E-to-Z isomerization about the C(15) = C(16) double bond between rings C and D is the initial photochemical event. As the chromophore relaxes, the twist of the C(15) methine bridge about its two dihedral angles is reversed. Structural changes extend further to rings B and A, and to the surrounding protein regions. These data indicate that absorption of a photon by the Pfr state of PaBphP converts a light signal into a structural signal via twisting and untwisting of the methine bridges in the linear tetrapyrrole within the confined protein cavity.
Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome.,Yang X, Ren Z, Kuk J, Moffat K Nature. 2011 Oct 16;479(7373):428-32. doi: 10.1038/nature10506. PMID:22002602[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang X, Ren Z, Kuk J, Moffat K. Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome. Nature. 2011 Oct 16;479(7373):428-32. doi: 10.1038/nature10506. PMID:22002602 doi:10.1038/nature10506
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