Voss N R, Gerstein M, Steitz T A, Moore P B
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
J Mol Biol. 2006 Jul 21;360(4):893-906. doi: 10.1016/j.jmb.2006.05.023. Epub 2006 May 30.
The geometry of the polypeptide exit tunnel has been determined using the crystal structure of the large ribosomal subunit from Haloarcula marismortui. The tunnel is a component of a much larger, interconnected system of channels accessible to solvent that permeates the subunit and is connected to the exterior at many points. Since water and other small molecules can diffuse into and out of the tunnel along many different trajectories, the large subunit cannot be part of the seal that keeps ions from passing through the ribosome-translocon complex. The structure referred to as the tunnel is the only passage in the solvent channel system that is both large enough to accommodate nascent peptides, and that traverses the particle. For objects of that size, it is effectively an unbranched tube connecting the peptidyl transferase center of the large subunit and the site where nascent peptides emerge. At no point is the tunnel big enough to accommodate folded polypeptides larger than alpha-helices.
利用嗜盐嗜碱菌(Haloarcula marismortui)大核糖体亚基的晶体结构,已确定了多肽出口通道的几何形状。该通道是一个更大的、相互连接的溶剂可及通道系统的组成部分,这些通道贯穿亚基并在多个点与外部相连。由于水和其他小分子可以沿着许多不同的轨迹扩散进出通道,大亚基不可能是阻止离子通过核糖体-转位酶复合物的密封结构的一部分。被称为通道的结构是溶剂通道系统中唯一既足够大以容纳新生肽,又贯穿颗粒的通道。对于该尺寸的物体,它实际上是一根连接大亚基肽基转移酶中心和新生肽出现位点的无分支管道。通道在任何位置都不够大,无法容纳大于α螺旋的折叠多肽。