3ENI

Crystal structure of the Fenna-Matthews-Olson Protein from Chlorobaculum Tepidum

「1M50」から置き換えられました 「1KSA」から置き換えられました

3ENI の概要

• エントリーDOI: 10.2210/pdb3eni/pdb
• 関連するPDBエントリー: 1KSA 1M50 3EOJ
• 分子名称: Bacteriochlorophyll a protein, BACTERIOCHLOROPHYLL A (3 entities in total)
• 機能のキーワード: beta sheet, gamma turn, bacteriochlorophyll, chlorophyll, chromophore, electron transport, magnesium, metal-binding, photosynthesis, reaction center, transport
• 由来する生物種: Chlorobaculum tepidum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95008.53

構造登録者

Tronrud, D.,Camara-Artigas, A.,Blankenship, R.,Allen, J.P. (登録日: 2008-09-25, 公開日: 2009-05-12, 最終更新日: 2024-02-21)

主引用文献

Tronrud, D.E.,Wen, J.,Gay, L.,Blankenship, R.E.
The structural basis for the difference in absorbance spectra for the FMO antenna protein from various green sulfur bacteria.
Photosynth.Res., 100:79-87, 2009

PubMed Abstract: The absorbance spectrum of the Fenna-Matthews-Olson protein--a component of the antenna system of Green Sulfur Bacteria--is always one of two types, depending on the species of the source organism. The FMO from Prosthecochloris aestuarii 2K has a spectrum of type 1 while that from Chlorobaculum tepidum is of type 2. The previously reported crystal structures for these two proteins did not disclose any rationale that would explain their spectral differences. We have collected a 1.3 A X-ray diffraction dataset of the FMO from Prosthecochloris aestuarii 2K, which has allowed us to identify an additional Bacteriochlorophyll-a molecule with chemical attachments to both sides of the central magnesium atom. A new analysis of the previously published X-ray data for the Chlorobaculum tepidum FMO shows the presence of a Bacteriochlorophyll-a molecule in an equivalent location but with a chemical attachment from only one side. This difference in binding is shown to be predictive of the spectral type of the FMO.

PubMed: 19437128
DOI: 10.1007/s11120-009-9430-6

実験手法

X-RAY DIFFRACTION (2.2 Å)