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9lzk
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The PSI1-IsiA13 complex with double-layered IsiA proteins bound to the monomeric PSI core== |
| + | <StructureSection load='9lzk' size='340' side='right'caption='[[9lzk]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9lzk]] is a 22 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=9LZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LZK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=LMU:DODECYL-ALPHA-D-MALTOSIDE'>LMU</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SQD:1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL'>SQD</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=9lzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9lzk OCA], [https://pdbe.org/9lzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9lzk RCSB], [https://www.ebi.ac.uk/pdbsum/9lzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9lzk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ISIA_THEVB ISIA_THEVB] Functions as an antenna for photosystem I (PSI) under iron-limiting conditions, when phycobilisomes disappear. In the (PSI)3(Isi3)18 complex most of the harvested energy is probably used by PSI; in other PSI-containing supercomplexes a large part of the energy will probably not be used for light harvesting, but rather is dissipated to protect the organism from light damage.[UniProtKB:Q55274] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Iron-limitation is a common stress factor in natural environments. To survive under iron-starved conditions, cyanobacteria overexpress iron stress-induced protein A (IsiA), which is crucial for light-harvesting and photoprotection. Multiple IsiA proteins form a single- or double-layered architecture encircling the photosystem I (PSI) core, forming various PSI-IsiA supercomplexes. The assembly and energy transfer mechanisms of double-layered PSI-IsiA supercomplexes remain unelucidated. Here, we present high-resolution structures of two PSI-IsiA supercomplexes isolated from the cyanobacterium Thermosynechococcus elongatus BP-1 cultured under iron-starved conditions. The PSI(3)-IsiA(43) complex contains a trimeric PSI core surrounded by 43 IsiA subunits assembled into a closed double-ring. The PSI(1)-IsiA(13) complex contains 13 IsiA proteins arranged in a double-layered architecture attached to the monomeric PSI core. Atomic force microscopy demonstrates the presence and distribution of different PSI-IsiA complexes within native thylakoid membranes isolated from iron-starved cells. Our findings provide insights into the structural variability and adaptive mechanisms of PSI-IsiA complexes. | ||
| - | + | Structural basis for the assembly and energy transfer between the cyanobacterial PSI core and the double-layered IsiA proteins.,Si L, Zhang Y, Su X, Zhao X, An X, Liu LN, Cao P, Li M Nat Commun. 2025 Dec 20. doi: 10.1038/s41467-025-67295-2. PMID:41422266<ref>PMID:41422266</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9lzk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermosynechococcus vestitus BP-1]] | ||
| + | [[Category: Cao P]] | ||
| + | [[Category: Li M]] | ||
| + | [[Category: Si L]] | ||
Current revision
The PSI1-IsiA13 complex with double-layered IsiA proteins bound to the monomeric PSI core
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