6uv8
From Proteopedia
(Difference between revisions)
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<StructureSection load='6uv8' size='340' side='right'caption='[[6uv8]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='6uv8' size='340' side='right'caption='[[6uv8]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UV8 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]] 2.701Å</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]] 2.701Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</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=6uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uv8 OCA], [https://pdbe.org/6uv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uv8 RCSB], [https://www.ebi.ac.uk/pdbsum/6uv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uv8 ProSAT]</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=6uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uv8 OCA], [https://pdbe.org/6uv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uv8 RCSB], [https://www.ebi.ac.uk/pdbsum/6uv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uv8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/K9ZI18_ANACC K9ZI18_ANACC] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cyanobacteriochromes (CBCRs) are small, linear tetrapyrrole (bilin)-binding photoreceptors in the phytochrome superfamily that regulate diverse light-mediated adaptive processes in cyanobacteria. More spectrally diverse than canonical red/far-red-sensing phytochromes, CBCRs were thought to be restricted to sensing visible and near UV light until recently when several subfamilies with far-red-sensing representatives (frCBCRs) were discovered. Two of these frCBCRs subfamilies have been shown to incorporate bilin precursors with larger pi-conjugated chromophores, while the third frCBCR subfamily uses the same phycocyanobilin precursor found in the bulk of the known CBCRs. To elucidate the molecular basis of far-red light perception by this third frCBCR subfamily, we determined the crystal structure of the far-red-absorbing dark state of one such frCBCR Anacy_2551g3 from Anabaena cylindrica PCC 7122 which exhibits a reversible far-red/orange photocycle. Determined by room temperature serial crystallography and cryocrystallography, the refined 2.7-A structure reveals an unusual all-Z,syn configuration of the phycocyanobilin (PCB) chromophore that is considerably less extended than those of previously characterized red-light sensors in the phytochrome superfamily. Based on structural and spectroscopic comparisons with other bilin-binding proteins together with site-directed mutagenesis data, our studies reveal protein-chromophore interactions that are critical for the atypical bathochromic shift. Based on these analyses, we propose that far-red absorption in Anacy_2551g3 is the result of the additive effect of two distinct red-shift mechanisms involving cationic bilin lactim tautomers stabilized by a constrained all-Z,syn conformation and specific interactions with a highly conserved anionic residue. | ||
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| - | Crystal structure of a far-red-sensing cyanobacteriochrome reveals an atypical bilin conformation and spectral tuning mechanism.,Bandara S, Rockwell NC, Zeng X, Ren Z, Wang C, Shin H, Martin SS, Moreno MV, Lagarias JC, Yang X Proc Natl Acad Sci U S A. 2021 Mar 23;118(12). pii: 2025094118. doi:, 10.1073/pnas.2025094118. PMID:33727422<ref>PMID:33727422</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6uv8" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Anabaena cylindrica PCC 7122]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bandara S]] | [[Category: Bandara S]] | ||
[[Category: Ren Z]] | [[Category: Ren Z]] | ||
[[Category: Yang X]] | [[Category: Yang X]] | ||
Current revision
Crystal structure of a far-red cyanobacteriochrome photoreceptor at room temperature
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