Structure of outer membrane protein G by solution NMR spectroscopy
Structure of outer membrane protein G by solution NMR spectroscopy
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DOI：
10.1073/pnas.0705466104
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发表时间：
2007-10-09
影响因子：
11.1
通讯作者：
Tamm, Lukas K.
中科院分区：
文献类型：
--
作者：
Liang, Binyong;Tamm, Lukas K.
细菌外膜蛋白 G (OmpG) 是一种单体 pH 门控孔蛋白，在大肠杆菌中过度表达，并在 β-辛基葡萄糖苷胶束中重折叠。转移到十二烷基磷酸胆碱胶束后，在 pH 6.3 下通过溶液 NMR 光谱测定 OmpG 的溶液结构。根据在 800 MHz 下一系列基于 TROSY 的 3D 实验确定的 CA、CB 和 CO 连接路径，获得了 280 个残基中的 234 个残基的完整主干分配。 14 链 β-桶的全局折叠是根据相邻链之间观察到的 133 个远程 NOE 以及局部化学位移和 NOE 信息确定的。桶的结构与以前的晶体结构非常相似，但溶液结构的循环相当灵活。
The bacterial outer membrane protein G (OmpG), a monomeric pH-gated porin, was overexpressed in Escherichia coli and refolded in beta-octyl glucoside micelles. After transfer into dodecylphosphocholine micelles, the solution structure of OmpG was determined by solution NMR spectroscopy at pH 6.3. Complete backbone assignments were obtained for 234 of 280 residues based on CA, CB, and CO connection pathways determined from a series of TROSY-based 3D experiments at 800 MHz. The global fold of the 14-stranded beta-barrel was determined based on 133 long-range NOEs observed between neighboring strands and local chemical shift and NOE information. The structure of the barrel is very similar to previous crystal structures, but the loops of the solution structure are quite flexible.