7ze8
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7ze8]] is a 19 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZE8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ze8]] is a 19 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZE8 FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXM:N-CARBOXYMETHIONINE'>CXM</scene>, <scene name='pdbligand=IRM:(6~{E},8~{E},10~{E},12~{E},14~{E},16~{E},18~{E},20~{E},22~{E},24~{E},26~{E})-2,6,10,14,19,23,27,31-octamethyldotriaconta-6,8,10,12,14,16,18,20,22,24,26,30-dodecaen-2-ol'>IRM</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=7ze8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ze8 OCA], [https://pdbe.org/7ze8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ze8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ze8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ze8 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=7ze8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ze8 OCA], [https://pdbe.org/7ze8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ze8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ze8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ze8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/Q6N9P5_RHOPA Q6N9P5_RHOPA] |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The genomes of some purple photosynthetic bacteria contain a multigene puc family encoding a series of alpha- and beta-polypeptides that together form a heterogeneous antenna of light-harvesting 2 (LH2) complexes. To unravel this complexity, we generated four sets of puc deletion mutants in Rhodopseudomonas palustris, each encoding a single type of pucBA gene pair and enabling the purification of complexes designated as PucA-LH2, PucB-LH2, PucD-LH2, and PucE-LH2. The structures of all four purified LH2 complexes were determined by cryogenic electron microscopy (cryo-EM) at resolutions ranging from 2.7 to 3.6 A. Uniquely, each of these complexes contains a hitherto unknown polypeptide, gamma, that forms an extended undulating ribbon that lies in the plane of the membrane and that encloses six of the nine LH2 alphabeta-subunits. The gamma-subunit, which is located near to the cytoplasmic side of the complex, breaks the C9 symmetry of the LH2 complex and binds six extra bacteriochlorophylls (BChls) that enhance the 800-nm absorption of each complex. The structures show that all four complexes have two complete rings of BChls, conferring absorption bands centered at 800 and 850 nm on the PucA-LH2, PucB-LH2, and PucE-LH2 complexes, but, unusually, the PucD-LH2 antenna has only a single strong near-infared (NIR) absorption peak at 803 nm. Comparison of the cryo-EM structures of these LH2 complexes reveals altered patterns of hydrogen bonds between LH2 alphabeta-side chains and the bacteriochlorin rings, further emphasizing the major role that H bonds play in spectral tuning of bacterial antenna complexes. | ||
| + | |||
| + | Cryo-EM structures of light-harvesting 2 complexes from Rhodopseudomonas palustris reveal the molecular origin of absorption tuning.,Qian P, Nguyen-Phan CT, Gardiner AT, Croll TI, Roszak AW, Southall J, Jackson PJ, Vasilev C, Castro-Hartmann P, Sader K, Hunter CN, Cogdell RJ Proc Natl Acad Sci U S A. 2022 Oct 25;119(43):e2210109119. doi: , 10.1073/pnas.2210109119. Epub 2022 Oct 17. PMID:36251992<ref>PMID:36251992</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ze8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
PucE-LH2 complex from Rps. palustris
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