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

被引：8
|
作者：
Boekema, EJ
Stuart, M
Koning, RI
Keegstra, W
Brisson, A
Verheij, HM
Dekker, N
机构：
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Dept Biophys Chem, NL-9747 AG Groningen, Netherlands
[2] Univ Utrecht, Biomembrane Inst, Dept Enzymol & Prot Engn, Ctr Biomembranes & Lipid Enzymol, Utrecht, Netherlands
来源：
JOURNAL OF STRUCTURAL BIOLOGY | 1998年 / 123卷 / 01期
关键词：
D O I：
10.1006/jsbi.1998.4013
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：
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-Angstrom projection map reveals OMPLA molecules exhibiting an oval-shaped domain of 30 x 20 Angstrom resembling the beta-barrel structure characteristic of porins, which is associated with a 25-Angstrom elongated domain of lower density. (C) 1998 Academic Press.
引用
收藏
页码：67 / 71
页数：5
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