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Expression, purification and preliminary crystallographic analysis of a haem-utilizing protein, HutX, from Vibrio

Tiantian Su1, Kaikai Chi1, Kang Wang1

  • 1State Key Laboratory of Microbial Technology, School of Life Science, Shandong University, 27 Shanda Nanlu, Jinan, Shandong 250100, People's Republic of China.

Acta Crystallographica. Section F, Structural Biology Communications
|February 10, 2015
PubMed

Vibrio cholerae, the causative agent of cholera, has developed a variety of mechanisms to obtain the limited-availability iron from human hosts. One important method for iron acquisition is through haem-uptake systems. Although the transport of haem has been widely studied, the fate of haem once it enters the cytoplasm remains an open question. Here, preliminary X-ray crystallographic analysis was performed on HutX, a member of the conserved haem-utilization operon from V. cholerae strain N16961. The crystals of HutX were found to belong to the orthorhombic space group C2221, with unit-cell parameters a = 50.1, b = 169.0, c = 81.8 Å. There are two protein molecules in the asymmetric unit, with a corresponding Matthews coefficient VM of 2.06 Å(3) Da(-1) and a solvent content of 40.28%.

Keywords:
Vibrio choleraehaem uptakeiron acquisition

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