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| <StructureSection load='6uvb' size='340' side='right'caption='[[6uvb]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='6uvb' size='340' side='right'caption='[[6uvb]], [[Resolution|resolution]] 3.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6uvb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_cylindrica_PCC_7122 Anabaena cylindrica PCC 7122]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UVB FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UVB 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]] 3Å</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='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=6uvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uvb OCA], [https://pdbe.org/6uvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uvb RCSB], [https://www.ebi.ac.uk/pdbsum/6uvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uvb 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=6uvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uvb OCA], [https://pdbe.org/6uvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uvb RCSB], [https://www.ebi.ac.uk/pdbsum/6uvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uvb ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
| |
| [https://www.uniprot.org/uniprot/K9ZI18_ANACC K9ZI18_ANACC]
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| <div style="background-color:#fffaf0;">
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| == 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6uvb" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Anabaena cylindrica PCC 7122]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Bandara S]] | | [[Category: Bandara S]] |
| [[Category: Ren Z]] | | [[Category: Ren Z]] |
| [[Category: Yang X]] | | [[Category: Yang X]] |
