Overproduction, purification and preliminary X-ray diffraction analysis of YncE, an iron-regulated Sec-dependent periplasmic protein from Escherichia coli

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2008-10, Vol.64 (10), p.966-969
• Main Authors: Baba-Dikwa, Aisha, Thompson, Darren, Spencer, Nick J., Andrews, Simon C., Watson, Kimberly A.
• Format: Article
• Language: English
• Subjects: Crystallization; Crystallization Communications; DNA Primers; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Fur; Iron; iron regulation; Methanosarcina mazei; Models, Molecular; periplasmic proteins; Polymerase Chain Reaction; Protein Conformation; TonB-dependent outer-membrane receptor; X-Ray Diffraction; YncE; β-propellers
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309108029515

The yncE gene of Escherichia coli encodes a predicted periplasmic protein of unknown function. The gene is de‐repressed under iron restriction through the action of the global iron regulator Fur. This suggests a role in iron acquisition, which is supported by the presence of the adjacent yncD gene encoding a potential TonB‐dependent outer‐membrane transporter. Here, the preliminary crystallographic structure of YncE is reported, revealing that it consists of a seven‐bladed β‐propeller which resembles the corresponding domain of the `surface‐layer protein' of Methanosarcina mazei. A full structure determination is under way in order to provide insight into the function of this protein.