Crystallization and preliminary X- ray crystallographic analysis of the curli transporter CsgG

被引：7

作者：

Goyal, Parveen ^{[1
,2
]}

Van Gerven, Nani ^{[1
,2
]}

Jonckheere, Wim ^{[1
,2
]}

Remaut, Han ^{[1
,2
]}

机构：

[1] VIB, VIB Dept Struct Biol, B-1050 Brussels, Belgium

[2] Vrije Univ Brussel, B-1050 Brussels, Belgium

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷

关键词：

ESCHERICHIA-COLI; OUTER-MEMBRANE; PROTEIN EXPORT; FIBRONECTIN-BINDING; AMYLOID FIBRILS; SECRETION; DISEASE; POLYMERIZATION; MECHANISMS; OPERONS;

D O I：

10.1107/S1744309113028054

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Gram-negative bacteria have eight known protein secretion systems. The type-VIII secretion system, also known as the curli biosynthesis system, is responsible for the formation of aggregative fibres known in Escherichia coli as curli. Curli are extracellular proteinaceous fibres primarily involved in bacterial biofilm formation and attachment to nonbiotic surfaces. The secretion of curli subunits depends on a dedicated lipoprotein, CsgG, which is found to form an oligomeric secretion channel in the outer membrane. A nonlipidated mutant of CsgG was expressed and crystallized in a soluble form. The crystals diffracted to 3.15 angstrom resolution and belong to space group P1 with a unit cell containing a predicted 16 molecules per asymmetric unit.

引用

页码：1349 / 1353

页数：5

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