SOLUTION CONFORMATION OF AN ANTIBACTERIAL PEPTIDE, SARCOTOXIN-IA, AS DETERMINED BY H-1-NMR
SOLUTION CONFORMATION OF AN ANTIBACTERIAL PEPTIDE, SARCOTOXIN-IA, AS DETERMINED BY H-1-NMR
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DOI：
10.1111/j.1432-1033.1993.tb18287.x
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发表时间：
1993-10-15
期刊：
影响因子：
--
通讯作者：
SHIMADA, I
中科院分区：
文献类型：
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作者：
IWAI, H;NAKAJIMA, Y;SHIMADA, I
用核磁共振波谱和混合距离几何/动态模拟退火法确定了肉毒素IA的溶液构象，该毒素是从Peregrina中分离得到的一种抗菌肽，分子质量为4 kDa。在227个实验约束的基础上，包括从NOE获得的185个距离约束和与21个氢键相关的42个约束，总共获得了18个肉瘤毒素IA的收敛结构。最终的18个收敛结构显示出主干-原子均方根差异，平均坐标位置为0.070+/-0.027 nm(残基3-23)和0.040+/-0.017 nm(残基28-38)。研究表明，结节毒素IA由螺旋I(Leu3-Gln23)和螺旋II(Ala28-Ala38)两个两亲性α-螺旋区组成，并有一个铰链区(Gly24-Ile27)连接螺旋I和螺旋II。我们认为这两个两亲性螺旋片段对表达抗菌活性具有重要意义。
The solution conformation of sarcotoxin IA, which is an antibacterial peptide isolated from Sarcophaga peregrina with a molecular mass of 4 kDa, was determined by NMR spectroscopy and hybrid distance geometry/dynamical simulated annealing calculations. On the basis of 227 experimental constraints, including 185 distance constraints obtained from NOE and 42 constraints associated with 21 hydrogen bonds, a total of 18 converged structures of sarcotoxin IA were obtained. The final 18 converged structures exhibit backbone-atomic root-mean-square differences about the averaged coordinate positions of 0.070 +/- 0.027 nm for residues 3 - 23 and 0.040 +/- 0.017 nm for residues 28-38. It has been indicated that sarcotoxin IA consists of two amphiphilic alpha-helical regions, i.e. helix I (Leu3 - Gln23) and helix II (Ala28 - Ala3 8), with a hinge region (Gly24 - Ile27), which connects helix I and helix II. We conclude that these two amphiphilic helical segments of sarcotoxin IA are of importance for the expression of the antibacterial activity.