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| | <StructureSection load='3vv4' size='340' side='right'caption='[[3vv4]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3vv4' size='340' side='right'caption='[[3vv4]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vv4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Theeb Theeb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VV4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vv4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VV4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PVG:PHYCOVIOLOBILIN,+GREEN+LIGHT-ABSORBING+FORM'>PVG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w2z|3w2z]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PVG:PHYCOVIOLOBILIN,+GREEN+LIGHT-ABSORBING+FORM'>PVG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tll0569 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB])</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=3vv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vv4 OCA], [https://pdbe.org/3vv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vv4 RCSB], [https://www.ebi.ac.uk/pdbsum/3vv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vv4 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=3vv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vv4 OCA], [https://pdbe.org/3vv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vv4 RCSB], [https://www.ebi.ac.uk/pdbsum/3vv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vv4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Theeb]] | + | [[Category: Thermosynechococcus vestitus BP-1]] |
| - | [[Category: Ikeuchi, M]] | + | [[Category: Ikeuchi M]] |
| - | [[Category: Ishizuka, T]] | + | [[Category: Ishizuka T]] |
| - | [[Category: Kurisu, G]] | + | [[Category: Kurisu G]] |
| - | [[Category: Muraki, N]] | + | [[Category: Muraki N]] |
| - | [[Category: Narikawa, R]] | + | [[Category: Narikawa R]] |
| - | [[Category: Shiba, T]] | + | [[Category: Shiba T]] |
| - | [[Category: Cyanobacteriochrome]]
| + | |
| - | [[Category: Phycoviolobilin binding]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Cyanobacteriochromes are cyanobacterial tetrapyrrole-binding photoreceptors that share a bilin-binding GAF domain with photoreceptors of the phytochrome family. Cyanobacteriochromes are divided into many subclasses with distinct spectral properties. Among them, putative phototaxis regulators PixJs of Anabaena sp. PCC 7120 and Thermosynechococcus elongatus BP-1 (denoted as AnPixJ and TePixJ, respectively) are representative of subclasses showing red-green-type and blue/green-type reversible photoconversion, respectively. Here, we determined crystal structures for the AnPixJ GAF domain in its red-absorbing 15Z state (Pr) and the TePixJ GAF domain in its green-absorbing 15E state (Pg). The overall structure of these proteins is similar to each other and also similar to known phytochromes. Critical differences found are as follows: (i) the chromophore of AnPixJ Pr is phycocyanobilin in a C5-Z,syn/C10-Z,syn/C15-Z,anti configuration and that of TePixJ Pg is phycoviolobilin in a C10-Z,syn/C15-E,anti configuration, (ii) a side chain of the key aspartic acid is hydrogen bonded to the tetrapyrrole rings A, B and C in AnPixJ Pr and to the pyrrole ring D in TePixJ Pg, (iii) additional protein-chromophore interactions are provided by subclass-specific residues including tryptophan in AnPixJ and cysteine in TePixJ. Possible structural changes following the photoisomerization of the chromophore between C15-Z and C15-E are discussed based on the X-ray structures at 1.8 and 2.0-A resolution, respectively, in two distinct configurations.
Structures of cyanobacteriochromes from phototaxis regulators AnPixJ and TePixJ reveal general and specific photoconversion mechanism.,Narikawa R, Ishizuka T, Muraki N, Shiba T, Kurisu G, Ikeuchi M Proc Natl Acad Sci U S A. 2013 Jan 15;110(3):918-23. doi:, 10.1073/pnas.1212098110. Epub 2012 Dec 19. PMID:23256156[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Narikawa R, Ishizuka T, Muraki N, Shiba T, Kurisu G, Ikeuchi M. Structures of cyanobacteriochromes from phototaxis regulators AnPixJ and TePixJ reveal general and specific photoconversion mechanism. Proc Natl Acad Sci U S A. 2013 Jan 15;110(3):918-23. doi:, 10.1073/pnas.1212098110. Epub 2012 Dec 19. PMID:23256156 doi:http://dx.doi.org/10.1073/pnas.1212098110
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