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

页码：67 / 71

页数：5

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