Overproduction, purification and preliminary X-ray diffraction analysis of YncE, an iron-regulated Sec-dependent periplasmic protein from Escherichia coliBaba-Dikwa, A., Thompson, D., Spencer, N. J., Andrews, S. C. ORCID: https://orcid.org/0000-0003-4295-2686 and Watson, K. A. ORCID: https://orcid.org/0000-0002-9987-8539 (2008) Overproduction, purification and preliminary X-ray diffraction analysis of YncE, an iron-regulated Sec-dependent periplasmic protein from Escherichia coli. Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 64. pp. 966-969. ISSN 1744-3091 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1107/s1744309108029515 Abstract/SummaryThe 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 beta-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.
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