Structure of outer membrane protein A transmembrane domain by NMR spectroscopy

被引：326

作者：

Arora, A

Abildgaard, F

Bushweller, JH

Tamm, LK ^{[1
]}

机构：

[1] Univ Virginia, Dept Mol Physiol & Biol Phys, Charlottesville, VA 22908 USA

[2] Univ Wisconsin, NMRFAM, Madison, WI 53706 USA

来源：

NATURE STRUCTURAL BIOLOGY | 2001年 / 8卷 / 04期

关键词：

D O I：

10.1038/86214

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have determined the three-dimensional fold of the 19 kDa (177 residues) transmembrane domain of the outer membrane protein A of Escherichia coli dodecylphosphocholine (DPC) micelles in solution using heteronuclear NMR. The structure consists of an eight-stranded beta -barrel connected by tight turns on the periplasmic side and larger mobile loops on the extracellular side. The solution structure of the barrel in DPC micelles is similar to that in n-octyltetraoxyethylene (C8E4) micelles determined by X-ray diffraction. Moreover, data from NMR dynamic experiments reveal a gradient of conformational flexibility in the structure that may contribute to the membrane channel function of this protein.

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页码：334 / 338

页数：5

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