5zoh: Difference between revisions
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==Crystal structure of a far-red light-absorbing form of AnPixJg2_BV4 in complex with biliverdin== | |||
<StructureSection load='5zoh' size='340' side='right'caption='[[5zoh]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5zoh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZOH 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]] 1.6Å</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5zoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoh OCA], [https://pdbe.org/5zoh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zoh RCSB], [https://www.ebi.ac.uk/pdbsum/5zoh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8YXY7_NOSS1 Q8YXY7_NOSS1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Because cyanobacteriochrome photoreceptors need only a single compact domain for chromophore incorporation and for absorption of visible spectra including the long-wavelength far-red region, these molecules have been paid much attention for application to bioimaging and optogenetics. Most cyanobacteriochromes, however, have a drawback to incorporate phycocyanobilin that is not available in the mammalian cells. In this study, we focused on biliverdin (BV) that is a mammalian intrinsic chromophore and absorbs the far-red region and revealed that replacement of only four residues was enough for conversion from BV-rejective cyanobacteriochromes into BV-acceptable molecules. We succeeded in determining the crystal structure of one of such engineered molecules, AnPixJg2_BV4, at 1.6 A resolution. This structure identified unusual covalent bond linkage, which resulted in deep BV insertion into the protein pocket. The four mutated residues contributed to reducing steric hindrances derived from the deeper insertion. We introduced these residues into other domains, and one of them, NpF2164g5_BV4, produced bright near-infrared fluorescence from mammalian liver in vivo. Collectively, this study provides not only molecular basis to incorporate BV by the cyanobacteriochromes but also rational strategy to open the door for application of cyanobacteriochromes to visualization and regulation of deep mammalian tissues. | |||
Rational conversion of chromophore selectivity of cyanobacteriochromes to accept mammalian intrinsic biliverdin.,Fushimi K, Miyazaki T, Kuwasaki Y, Nakajima T, Yamamoto T, Suzuki K, Ueda Y, Miyake K, Takeda Y, Choi JH, Kawagishi H, Park EY, Ikeuchi M, Sato M, Narikawa R Proc Natl Acad Sci U S A. 2019 Apr 4. pii: 1818836116. doi:, 10.1073/pnas.1818836116. PMID:30948637<ref>PMID:30948637</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5zoh" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Nostoc sp. PCC 7120 = FACHB-418]] | |||
[[Category: Fushimi K]] | |||
[[Category: Miyazaki T]] | |||
[[Category: Narikawa R]] | |||
Latest revision as of 12:02, 22 November 2023
Crystal structure of a far-red light-absorbing form of AnPixJg2_BV4 in complex with biliverdinCrystal structure of a far-red light-absorbing form of AnPixJg2_BV4 in complex with biliverdin
Structural highlights
FunctionPublication Abstract from PubMedBecause cyanobacteriochrome photoreceptors need only a single compact domain for chromophore incorporation and for absorption of visible spectra including the long-wavelength far-red region, these molecules have been paid much attention for application to bioimaging and optogenetics. Most cyanobacteriochromes, however, have a drawback to incorporate phycocyanobilin that is not available in the mammalian cells. In this study, we focused on biliverdin (BV) that is a mammalian intrinsic chromophore and absorbs the far-red region and revealed that replacement of only four residues was enough for conversion from BV-rejective cyanobacteriochromes into BV-acceptable molecules. We succeeded in determining the crystal structure of one of such engineered molecules, AnPixJg2_BV4, at 1.6 A resolution. This structure identified unusual covalent bond linkage, which resulted in deep BV insertion into the protein pocket. The four mutated residues contributed to reducing steric hindrances derived from the deeper insertion. We introduced these residues into other domains, and one of them, NpF2164g5_BV4, produced bright near-infrared fluorescence from mammalian liver in vivo. Collectively, this study provides not only molecular basis to incorporate BV by the cyanobacteriochromes but also rational strategy to open the door for application of cyanobacteriochromes to visualization and regulation of deep mammalian tissues. Rational conversion of chromophore selectivity of cyanobacteriochromes to accept mammalian intrinsic biliverdin.,Fushimi K, Miyazaki T, Kuwasaki Y, Nakajima T, Yamamoto T, Suzuki K, Ueda Y, Miyake K, Takeda Y, Choi JH, Kawagishi H, Park EY, Ikeuchi M, Sato M, Narikawa R Proc Natl Acad Sci U S A. 2019 Apr 4. pii: 1818836116. doi:, 10.1073/pnas.1818836116. PMID:30948637[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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