8YPB
Cryo-EM structure of the LH1 complex from Allochromatium tepidum
8YPB の概要
エントリーDOI | 10.2210/pdb8ypb/pdb |
EMDBエントリー | 39475 |
分子名称 | Beta subunit of light-harvesting 1 complex, LH1 alpha polypeptide, BACTERIOCHLOROPHYLL A, ... (5 entities in total) |
機能のキーワード | lh1 complex, photosynthesis |
由来する生物種 | Allochromatium tepidum 詳細 |
タンパク質・核酸の鎖数 | 28 |
化学式量合計 | 210445.80 |
構造登録者 | |
主引用文献 | Zou, M.J.,Sun, S.,Wang, G.L.,Yan, Y.H.,Ji, W.,Wang-Otomo, Z.Y.,Madigan, M.T.,Yu, L.J. Probing the Dual Role of Ca 2+ in the Allochromatium tepidum LH1-RC Complex by Constructing and Analyzing Ca 2+ -Bound and Ca 2+ -Free LH1 Complexes. Biomolecules, 15:-, 2025 Cited by PubMed Abstract: The genome of the mildly thermophilic hot spring purple sulfur bacterium, (.) , contains a multigene family that encodes a series of α- and β-polypeptides, collectively forming a heterogeneous light-harvesting 1 (LH1) complex. The LH1, therefore, offers a unique model for studying an intermediate phenotype between phototrophic thermophilic and mesophilic bacteria, particularly regarding their LH1 transition and moderately enhanced thermal stability. Of the 16 α-polypeptides in the LH1, six α1 bind Ca to connect with β1- or β3-polypeptides in specific Ca-binding sites. Here, we use the purple bacterium strain H2 as a host to express Ca-bound and Ca-free LH1-only complexes composed of α- and β-polypeptides that either contain or lack the calcium-binding motif WxxDxI; purified preparations of each complex were then used to test how Ca affects their thermostability and spectral features. The cryo-EM structures of both complexes were closed circular rings consisting of 14 αβ-polypeptides. The absorption maximum of Ca-bound LH1 (α1/β1 and α1/β3) was at 894 nm, while that of Ca-free (α2/β1) was at 888 nm, indicating that Ca imparts a transition of 6 nm. Crucially for the ecological success of , Ca-bound LH1 complexes were more thermostable than Ca-free complexes, indicating that calcium plays at least two major roles in photosynthesis by -improving photocomplex stability and modifying its spectrum. PubMed: 39858518DOI: 10.3390/biom15010124 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.45 Å) |
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