5y5s
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/D2Z0P1_THETI D2Z0P1_THETI]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers (By similarity).[SAAS:SAAS000066_004_008786] [[http://www.uniprot.org/uniprot/CYCR_THETI CYCR_THETI]] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.[PIRNR:PIRNR000017] [[http://www.uniprot.org/uniprot/D2Z0P2_THETI D2Z0P2_THETI]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers (By similarity).[SAAS:SAAS000066_004_008786] | [[http://www.uniprot.org/uniprot/D2Z0P1_THETI D2Z0P1_THETI]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers (By similarity).[SAAS:SAAS000066_004_008786] [[http://www.uniprot.org/uniprot/CYCR_THETI CYCR_THETI]] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.[PIRNR:PIRNR000017] [[http://www.uniprot.org/uniprot/D2Z0P2_THETI D2Z0P2_THETI]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers (By similarity).[SAAS:SAAS000066_004_008786] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Light-harvesting complex 1 (LH1) and the reaction centre (RC) form a membrane-protein supercomplex that performs the primary reactions of photosynthesis in purple photosynthetic bacteria. The structure of the LH1-RC complex can provide information on the arrangement of protein subunits and cofactors; however, so far it has been resolved only at a relatively low resolution. Here we report the crystal structure of the calcium-ion-bound LH1-RC supercomplex of Thermochromatium tepidum at a resolution of 1.9 A. This atomic-resolution structure revealed several new features about the organization of protein subunits and cofactors. We describe the loop regions of RC in their intact states, the interaction of these loop regions with the LH1 subunits, the exchange route for the bound quinone QB with free quinone molecules, the transport of free quinones between the inside and outside of the LH1 ring structure, and the detailed calcium-ion-binding environment. This structure provides a solid basis for the detailed examination of the light reactions that occur during bacterial photosynthesis. | ||
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| + | Structure of photosynthetic LH1-RC supercomplex at 1.9 A resolution.,Yu LJ, Suga M, Wang-Otomo ZY, Shen JR Nature. 2018 Apr;556(7700):209-213. doi: 10.1038/s41586-018-0002-9. Epub 2018 Apr, 4. PMID:29618814<ref>PMID:29618814</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5y5s" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Thermochromatium tepidum]] | [[Category: Thermochromatium tepidum]] | ||
| - | [[Category: Otomo-Wang, Z Y]] | ||
[[Category: Shen, J R]] | [[Category: Shen, J R]] | ||
[[Category: Suga, M]] | [[Category: Suga, M]] | ||
| + | [[Category: Wang-Otomo, Z Y]] | ||
[[Category: Yu, L J]] | [[Category: Yu, L J]] | ||
[[Category: Lh1-rc]] | [[Category: Lh1-rc]] | ||
[[Category: Photosynthesis]] | [[Category: Photosynthesis]] | ||
[[Category: Purple bacteria]] | [[Category: Purple bacteria]] | ||
Revision as of 05:55, 25 April 2018
Structure of photosynthetic LH1-RC super-complex at 1.9 angstrom resolution
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