The gramicidin pore: crystal structure of a cesium complex.
The gramicidin pore: crystal structure of a cesium complex.
复制标题
短杆菌肽孔：铯络合物的晶体结构。
作者：
B. Wallace;K. Ravikumar
Gramicidin是一种线性多肽，由L-和D-构型交替的疏水氨基酸组成，形成跨膜离子通道。gramicide -铯配合物的晶体结构在2.0埃分辨率下被确定。在这个结构中，革兰杀菌素形成了一个26埃长的管，由两条多肽链组成，这些多肽链排列成反平行的β链，它们被包裹成一个左旋螺旋线圈，每转6.4个残基。多肽主链形成亲水的、充满溶剂的孔的内部，而侧链在孔的外部形成疏水的、相对规则的表面。这个充满溶剂的离子孔晶体结构的例子为理解离子移位的物理性质提供了基础。
Gramicidin, a linear polypeptide composed of hydrophobic amino acids with alternating L- and D- configurations, forms transmembrane ion channels. The crystal structure of a gramicidin-cesium complex has been determined at 2.0 angstrom resolution. In this structure, gramicidin forms a 26 angstrom long tube comprised of two polypeptide chains arranged as antiparallel beta strands that are wrapped into a left-handed helical coil with 6.4 residues per turn. The polypeptide backbone forms the interior of the hydrophilic, solvent-filled pore and the side chains form a hydrophobic and relatively regular surface on the outside of the pore. This example of a crystal structure of a solvent-filled ion pore provides a basis for understanding the physical nature of ion translocation.
影响因子：
--
作者：
Wayne A. Hendrickson;Janet L. Smith;Steven Sheriff
通讯作者：
Wayne A. Hendrickson;Janet L. Smith;Steven Sheriff
为什么短杆菌肽具有价态选择性？
影响因子：
3.4
作者：
Sung,SS;Jordan,PC
通讯作者：
Jordan,PC