Premium
Expression, purification, crystallization and X‐ray crystallographic analysis of the periplasmic binding protein VatD from Vibrio vulnificus M2799
Author(s) -
Miyano Nao,
Igarashi Tomoko,
Kawano Hiroaki,
Miyamoto Katsushiro,
Tsuchiya Takahiro,
Tomoo Koji,
Tsujibo Hiroshi
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15011759
Subject(s) - periplasmic space , vibrio vulnificus , crystallization , halophile , crystal (programming language) , crystallography , chemistry , binding protein , microbiology and biotechnology , bacteria , biology , biochemistry , escherichia coli , genetics , gene , computer science , programming language , organic chemistry
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 P 6 4 22, while the crystal of the VatD–FOB complex belonged to space group P 2 1 . The difference in the two crystal forms could be caused by the binding of FOB to VatD.