Reinterpretation of the electron density at the site of the eighth bacteriochlorophyll in the FMO protein from Pelodictyon phaeum.

Reinterpretation of the electron density at the site of the eighth bacteriochlorophyll in the FMO protein from Pelodictyon phaeum.
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DOI:
10.1007/s11120-012-9735-8
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发表时间:
2012-04
影响因子:
3.7
通讯作者:
Allen, James P.
Allen, James P.
中科院分区:
生物学3区
文献类型:
--
作者:
Tronrud, Dale E.;Allen, James P.

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来自绿色细菌Pelodictyon phaeum的Fenna-Matthews-Olson天线蛋白介导了从外围天线复合体到膜结合反应中心的能量转移。这种蛋白质的三维结构以前已经用X射线衍射进行了模拟,分辨率极限为2.0ä,Rwork和Rfred值分别为16.6%和19.9%(Photosyn res 107:139-150)。这个模型显示蛋白质是由围绕着几个细菌-叶绿素辅助因子的β-Sheet组成的。虽然大多数模型与电子密度图明显匹配,但在本文中,我们重新检查了电子密度的一个特定特征,即第八个细菌叶绿素a辅因子。这种电子密度现在被解释为主要来自于一个原本无序的聚乙二醇分子的末端。存在额外的电子密度,但密度很弱,不能明确指定。新模型的Rwork和Rfred值分别为16.2%和19.0%。
The Fenna-Matthews-Olson antenna protein from the green bacterium Pelodictyon phaeum mediates the energy transfer from a peripheral antenna complex to the membrane-bound reaction center. The three-dimensional structure of this protein has been previously modeled using X-ray diffraction to a resolution limit of 2.0 Å, with Rwork and Rfree values of 16.6% and 19.9% respectively ( Photosyn Res 107: 139–150). This model shows the protein as consisting of β-sheets surrounding several bacteriochlorophyll cofactors. While most of the model clearly matches the electron density maps, in this paper we re-examine the electron density for a specific feature, namely the eighth bacteriochlorophyll a cofactor. This electron density is now interpreted as arising primarily from the end of an otherwise disordered polyethylene glycol molecule. Additional electron density is present but the density is weak and cannot be unambiguously assigned. The new model has Rwork and Rfree values of 16.2% and 19.0%, respectively.
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