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| | ==Crystal structure of the Bilin-binding domain of phycobilisome core-membrane linker ApcE== | | ==Crystal structure of the Bilin-binding domain of phycobilisome core-membrane linker ApcE== |
| - | <StructureSection load='4xxi' size='340' side='right' caption='[[4xxi]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4xxi' size='340' side='right'caption='[[4xxi]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xxi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XXI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XXI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xxi]] is a 2 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=4XXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XXI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xxk|4xxk]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">apcE, alr0020 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Anabaena 7120])</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=4xxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xxi OCA], [https://pdbe.org/4xxi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xxi RCSB], [https://www.ebi.ac.uk/pdbsum/4xxi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xxi ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xxi OCA], [http://pdbe.org/4xxi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xxi RCSB], [http://www.ebi.ac.uk/pdbsum/4xxi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xxi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/APCE_NOSS1 APCE_NOSS1]] This protein is postulated to act both as terminal energy acceptor (by its phycobilin-like domains) and as a linker polypeptide (by its repeats and arms) that stabilizes the phycobilisome core architecture. Has intrinsic bilin lyase activity (By similarity). | + | [https://www.uniprot.org/uniprot/APCE_NOSS1 APCE_NOSS1] This protein is postulated to act both as terminal energy acceptor (by its phycobilin-like domains) and as a linker polypeptide (by its repeats and arms) that stabilizes the phycobilisome core architecture. Has intrinsic bilin lyase activity (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anabaena 7120]] | + | [[Category: Large Structures]] |
| - | [[Category: Ding, W L]] | + | [[Category: Nostoc sp. PCC 7120 = FACHB-418]] |
| - | [[Category: Gartner, W]] | + | [[Category: Ding W-L]] |
| - | [[Category: Hoppner, A]] | + | [[Category: Gartner W]] |
| - | [[Category: Tang, K]] | + | [[Category: Hoppner A]] |
| - | [[Category: Zhao, K H]] | + | [[Category: Tang K]] |
| - | [[Category: Apce]]
| + | [[Category: Zhao K-H]] |
| - | [[Category: Phycobilisome]]
| + | |
| - | [[Category: Phycocyanobilin attachment]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
APCE_NOSS1 This protein is postulated to act both as terminal energy acceptor (by its phycobilin-like domains) and as a linker polypeptide (by its repeats and arms) that stabilizes the phycobilisome core architecture. Has intrinsic bilin lyase activity (By similarity).
Publication Abstract from PubMed
Photosynthesis relies on energy transfer from light-harvesting complexes to reaction centers. Phycobilisomes, the light-harvesting antennas in cyanobacteria and red algae, attach to the membrane via the multidomain core-membrane linker, LCM. The chromophore domain of LCM forms a bottleneck for funneling the harvested energy either productively to reaction centers or, in case of light overload, to quenchers like orange carotenoid protein (OCP) that prevent photodamage. The crystal structure of the solubly modified chromophore domain from Nostoc sp. PCC7120 was resolved at 2.2 A. Although its protein fold is similar to the protein folds of phycobiliproteins, the phycocyanobilin (PCB) chromophore adopts ZZZssa geometry, which is unknown among phycobiliproteins but characteristic for sensory photoreceptors (phytochromes and cyanobacteriochromes). However, chromophore photoisomerization is inhibited in LCM by tight packing. The ZZZssa geometry of the chromophore and pi-pi stacking with a neighboring Trp account for the functionally relevant extreme spectral red shift of LCM. Exciton coupling is excluded by the large distance between two PCBs in a homodimer and by preservation of the spectral features in monomers. The structure also indicates a distinct flexibility that could be involved in quenching. The conclusions from the crystal structure are supported by femtosecond transient absorption spectra in solution.
The terminal phycobilisome emitter, LCM: A light-harvesting pigment with a phytochrome chromophore.,Tang K, Ding WL, Hoppner A, Zhao C, Zhang L, Hontani Y, Kennis JT, Gartner W, Scheer H, Zhou M, Zhao KH Proc Natl Acad Sci U S A. 2015 Dec 29;112(52):15880-5. doi:, 10.1073/pnas.1519177113. Epub 2015 Dec 15. PMID:26669441[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tang K, Ding WL, Hoppner A, Zhao C, Zhang L, Hontani Y, Kennis JT, Gartner W, Scheer H, Zhou M, Zhao KH. The terminal phycobilisome emitter, LCM: A light-harvesting pigment with a phytochrome chromophore. Proc Natl Acad Sci U S A. 2015 Dec 29;112(52):15880-5. doi:, 10.1073/pnas.1519177113. Epub 2015 Dec 15. PMID:26669441 doi:http://dx.doi.org/10.1073/pnas.1519177113
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