通过电子晶体学解析的大肠杆菌外膜磷脂酶A的7.4 Å投影结构。

A 7.4-A projection structure of outer membrane phospholipase A from Escherichia coli by electron crystallography.

作者信息

Boekema E J, Stuart M, Koning R I, Keegstra W, Brisson A, Verheij H M, Dekker N

机构信息

Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, Groningen, NL-9747 AG, The Netherlands.

出版信息

J Struct Biol. 1998 Sep;123(1):67-71. doi: 10.1006/jsbi.1998.4013.

DOI:10.1006/jsbi.1998.4013

PMID:9774546

Abstract

Outer membrane phospholipase A (OMPLA) is one of the few enzymes present in the outer membrane of Escherichia coli. Two-dimensional crystals of OMPLA were grown by reconstitution of purified protein into lipid bilayers via detergent dialysis and were studied by electron crystallography. A 7.4-A projection map reveals OMPLA molecules exhibiting an oval-shaped domain of 30 x 20 A resembling the beta-barrel structure characteristic of porins, which is associated with a 25-A elongated domain of lower density.

摘要

外膜磷脂酶A（OMPLA）是存在于大肠杆菌外膜中的少数几种酶之一。通过去污剂透析将纯化的蛋白质重组到脂质双层中来生长OMPLA的二维晶体，并通过电子晶体学进行研究。一幅7.4埃的投影图显示，OMPLA分子呈现出一个30×20埃的椭圆形结构域，类似于孔蛋白的β桶结构特征，该结构域与一个25埃的低密度延长结构域相关联。