Crystallization and preliminary X-ray analysis of the C-terminal fragment of PorM, a subunit of the Porphyromonas gingivalis type IX secretion system

被引：6

作者：

Stathopulos, Julien ^{[1
,2
]}

Cambillau, Christian ^{[1
,2
]}

Cascales, Eric ^{[2
,3
]}

Roussel, Alain ^{[1
,2
]}

Leone, Philippe ^{[1
,2
]}

机构：

[1] UMR 7257 CNRS, Marseille, France

[2] Aix Marseille Univ, Marseille, France

[3] UMR 7255 CNRS, LISM, Marseille, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2015年 / 71卷

关键词：

Porphyromonas gingivalis; T9SS; OUTER-MEMBRANE PROTEIN; GLIDING MOTILITY; DATA QUALITY; GINGIPAINS; CRYSTALS; PATHOGEN; MODEL;

D O I：

10.1107/S2053230X1402559X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

PorM is a membrane protein involved in the assembly of the type IX secretion system (T9SS) from Porphyromonas gingivalis, a major bacterial pathogen responsible for periodontal disease in humans. The periplasmic domain of PorM was overexpressed in Escherichia coli and purified. A fragment of the purified protein was obtained by limited proteolysis. Crystals of this fragment belonged to the tetragonal space group P4(3)2(1)2. Native and MAD data sets were recorded to 2.85 and 3.1 angstrom resolution, respectively, using synchrotron radiation.

引用

页码：71 / 74

页数：4

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