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


ABSTRACT: 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-Fe(3+) (VatD-FOB) complex were obtained. The crystal of apo VatD belonged to space group P6422, while the crystal of the VatD-FOB complex belonged to space group P21. The difference in the two crystal forms could be caused by the binding of FOB to VatD.

SUBMITTER: Miyano N 

PROVIDER: S-EPMC4528945 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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

Miyano Nao N   Igarashi Tomoko T   Kawano Hiroaki H   Miyamoto Katsushiro K   Tsuchiya Takahiro T   Tomoo Koji K   Tsujibo Hiroshi H  

Acta crystallographica. Section F, Structural biology communications 20150729 Pt 8


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-Fe(3+) (VatD-FOB) complex were obtained. The cryst  ...[more]

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