6xhh

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Current revision (11:23, 30 October 2024) (edit) (undo)
 
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<StructureSection load='6xhh' size='340' side='right'caption='[[6xhh]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='6xhh' size='340' side='right'caption='[[6xhh]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6xhh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptolyngbya_sp._JSC-1 Leptolyngbya sp. JSC-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XHH FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XHH 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]] 1.5&#8491;</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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M1V:MESOBILIVERDIN+IX(ALPHA)'>M1V</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M1V:MESOBILIVERDIN+IX(ALPHA)'>M1V</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=6xhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xhh OCA], [https://pdbe.org/6xhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xhh RCSB], [https://www.ebi.ac.uk/pdbsum/6xhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xhh 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=6xhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xhh OCA], [https://pdbe.org/6xhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xhh RCSB], [https://www.ebi.ac.uk/pdbsum/6xhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xhh ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Cyanobacteriochromes (CBCRs) are photoswitchable linear tetrapyrrole (bilin)-based light sensors in the phytochrome superfamily with a broad spectral range from the near UV through the far red (330 to 760 nm). The recent discovery of far-red absorbing CBCRs (frCBCRs) has garnered considerable interest from the optogenetic and imaging communities because of the deep penetrance of far-red light into mammalian tissue and the small size of the CBCR protein scaffold. The present studies were undertaken to determine the structural basis for far-red absorption by JSC1_58120g3, a frCBCR from the thermophilic cyanobacterium Leptolyngbya sp. JSC-1 that is a representative member of a phylogenetically distinct class. Unlike most CBCRs that bind phycocyanobilin (PCB), a phycobilin naturally occurring in cyanobacteria and only a few eukaryotic phototrophs, JSC1_58120g3's far-red absorption arises from incorporation of the PCB biosynthetic intermediate 18(1),18(2)-dihydrobiliverdin (18(1),18(2)-DHBV) rather than the more reduced and more abundant PCB. JSC1_58120g3 can also yield a far-red-absorbing adduct with the more widespread linear tetrapyrrole biliverdin IXalpha (BV), thus circumventing the need to coproduce or supplement optogenetic cell lines with PCB. Using high-resolution X-ray crystal structures of 18(1),18(2)-DHBV and BV adducts of JSC1_58120g3 along with structure-guided mutagenesis, we have defined residues critical for its verdin-binding preference and far-red absorption. Far-red sensing and verdin incorporation make this frCBCR lineage an attractive template for developing robust optogenetic and imaging reagents for deep tissue applications.
 
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A far-red cyanobacteriochrome lineage specific for verdins.,Moreno MV, Rockwell NC, Mora M, Fisher AJ, Lagarias JC Proc Natl Acad Sci U S A. 2020 Oct 26. pii: 2016047117. doi:, 10.1073/pnas.2016047117. PMID:33106421<ref>PMID:33106421</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 6xhh" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Ribosome 3D structures|Ribosome 3D structures]]
*[[Ribosome 3D structures|Ribosome 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
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</StructureSection>
</StructureSection>

Current revision

Far-red absorbing dark state of JSC1_58120g3 with bound 18-1, 18-2 dihydrobiliverdin IXa (DHBV), the native chromophore precursor

PDB ID 6xhh

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