Structure of the PduU shell protein from the Pdu microcompartment of Salmonella.
Structure of the PduU shell protein from the Pdu microcompartment of Salmonella.
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DOI：
10.1016/j.str.2008.05.013
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发表时间：
2008-09-10
期刊：
影响因子：
--
通讯作者：
Yeates TO
中科院分区：
文献类型：
--
作者：
Crowley CS;Sawaya MR;Bobik TA;Yeates TO
Pdu微区室是一种蛋白质亚细胞结构，作为肠道沙门氏菌中1，2-丙二醇代谢的细胞器。它将几种相关的酶包裹在由几千个蛋白质亚基组成的外壳内。最近的结构研究的羧基体，一个相关的微区室参与CO2固定，得出的结论是，主要的壳蛋白从该微区室形成六聚体，包装成层，包括小平面的外壳。在这里，我们报告的晶体结构的PduU，蛋白质的Pdu微室，代表的第一个结构的壳蛋白从一个非羧基体微室。虽然PduU是一个六聚体像其他特征的壳蛋白，它经历了一个循环排列，导致显着的差异，在六聚体孔。鉴于微区室代谢物通过这些孔扩散穿过外壳的假设，PduU的独特结构表明可能具有特殊的功能作用。
The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in Salmonella enterica. It encapsulates several related enzymes within a shell composed of a few thousand protein subunits. Recent structural studies on the carboxysome, a related microcompartment involved in CO2 fixation, have concluded that the major shell proteins from that microcompartment form hexamers that pack into layers comprising the facets of the shell. Here we report the crystal structure of PduU, a protein from the Pdu microcompartment, representing the first structure of a shell protein from a non-carboxysome microcompartment. While PduU is a hexamer like other characterized shell proteins, it has undergone a circular permutation leading to dramatic differences in the hexamer pore. In view of the hypothesis that microcompartment metabolites diffuse across the outer shell through these pores, the unique structure of PduU suggests the possibility of a special functional role.
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影响因子：
8
作者：
COLOVOS, C;YEATES, TO
通讯作者：
YEATES, TO
影响因子：
3.2
作者：
Johnson, CLV;Pechonick, E;Bobik, TA
通讯作者：
Bobik, TA
DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
影响因子：
3.2
作者：
Havemann, GD;Sampson, EM;Bobik, TA
通讯作者：
Bobik, TA
影响因子：
56.9
作者：
Kerfeld, CA;Sawaya, MR;Yeates, TO
通讯作者：
Yeates, TO