白色链霉菌G的β-内酰胺酶在0.3纳米分辨率下的晶体结构。
The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution.
作者信息
Dideberg O, Charlier P, Wéry J P, Dehottay P, Dusart J, Erpicum T, Frère J M, Ghuysen J M
机构信息
Laboratoire de Cristalographie, Institut de Physique, University of Liège, Belgium.
出版信息
Biochem J. 1987 Aug 1;245(3):911-3. doi: 10.1042/bj2450911.
Abstract
The crystal structure of the beta-lactamase of Streptomyces albus G has been solved at 0.3 nm resolution by X-ray-diffraction methods. The enzyme is a typical two-domain protein. One domain consists of five alpha-helices, and the other is five-stranded beta-sheet with alpha-helices on both sides of the sheet. The active-site serine residue (Ser-48) is within a cleft located between the two domains.
摘要
通过X射线衍射方法，已解析出白色链霉菌G的β-内酰胺酶的晶体结构，分辨率为0.3纳米。该酶是一种典型的双结构域蛋白。一个结构域由五个α螺旋组成，另一个是五链β折叠，在折叠两侧均有α螺旋。活性位点丝氨酸残基（Ser-48）位于两个结构域之间的裂隙内。
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