Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum.
Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum.
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来自超嗜热古菌嗜气热杆菌的多铜氧化酶的结构。
DOI：
10.1107/s1744309111018173
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
T. Ohshima
中科院分区：
文献类型：
--
作者：
H. Sakuraba;Kohtaroh Koga;K. Yoneda;Y. Kashima;T. Ohshima
从嗜热古细菌中分离出一种极耐热的多铜氧化酶(MCoP)，其晶体结构的分辨率为2.0 ä。整个折叠由三个铜还蛋白样区组成，主链坐标与来自大肠杆菌(CueO)和枯草芽孢杆菌(Cota)的多铜氧化酶相似。然而，McoP与其他两种酶在结构域3附近有明显的拓扑差异：在CueO中不存在甲硫氨酸丰富的螺旋，在Cota中不存在突出的螺旋。相反，一个大的环(PL-1)覆盖了MCoP的T1铜中心，并在PL-1的N端附近的结构域3中延伸了一个短的α-螺旋。此外，MCoP中的几个表面环的尺寸明显小于CueO和CoTa中的相应环。结构比较表明，存在广泛的疏水相互作用和较小的空腔体积可能是导致MCoP超热稳定性的主要因素。
The crystal structure of an extremely thermostable multicopper oxidase (McoP) from the hyperthermophilic archaeon Pyrobaculum aerophilum was determined at a resolution of 2.0 Å. The overall fold was comprised of three cupredoxin-like domains and the main-chain coordinates of the enzyme were similar to those of multicopper oxidases from Escherichia coli (CueO) and Bacillus subtilis (CotA). However, there were clear topological differences around domain 3 between McoP and the other two enzymes: a methionine-rich helix in CueO and a protruding helix in CotA were not present in McoP. Instead, a large loop (PL-1) covered the T1 copper centre of McoP and a short α-helix in domain 3 extended near the N-terminal end of PL-1. In addition, the sizes of several surface loops in McoP were markedly smaller than the corresponding loops in CueO and CotA. Structural comparison revealed that the presence of extensive hydrophobic interactions and a smaller cavity volume are likely to be the main factors contributing to the hyperthermostability of McoP.
DOI：
10.1002/prot.10286
发表时间：
2003-02-15
期刊：
PROTEINS-STRUCTURE FUNCTION AND GENETICS
影响因子：
--
作者：
Lovell, SC;Davis, IW;Richardson, DC
通讯作者：
Richardson, DC
影响因子：
5.6
作者：
Bhuiya, MW;Sakuraba, H;Tsuge, H
通讯作者：
Tsuge, H