Expression, purification, crystallization and X-ray crystallographic analysis of the periplasmic binding protein VatD from Vibrio vulnificus M2799

被引：2
|
作者：
Miyano, Nao [1 ]
Igarashi, Tomoko [1 ]
Kawano, Hiroaki [1 ]
Miyamoto, Katsushiro [1 ]
Tsuchiya, Takahiro [1 ]
Tomoo, Koji [2 ]
Tsujibo, Hiroshi [1 ]
机构：
[1] Osaka Univ Pharmaceut Sci, Dept Microbiol, Takatsuki, Osaka 5691094, Japan
[2] Osaka Univ Pharmaceut Sci, Dept Phys Chem, Takatsuki, Osaka 5691094, Japan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2015年 / 71卷
关键词：
Vibrio vulnificus; periplasmic binding protein; siderophore; iron; desferrioxamine B; VULNIBACTIN; SIDEROPHORE; INFECTIONS; VIRULENCE; FEATURES; SYSTEM;
D O I：
10.1107/S2053230X15011759
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Vibrio vulnificus is a halophilic marine microorganism which causes gastroenteritis and primary septicaemia in humans. An important factor that determines the survival of V. vulnificus in the human body is its ability to acquire iron. VatD is a periplasmic siderophore-binding protein from V. vulnificus M2799. The current study reports the expression, purification and crystallization of VatD. Crystals of both apo VatD and a VatD-desferrioxamine B-Fe3+ (VatD-FOB) complex were obtained. The crystal of apo VatD belonged to space group P6(4)22, while the crystal of the VatD-FOB complex belonged to space group P2(1). The difference in the two crystal forms could be caused by the binding of FOB to VatD.
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收藏
页码：1078 / 1082
页数：5
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