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Preliminary X-ray diffraction analysis of YcdB from Escherichia coli: a novel haem-containing and Tat-secreted periplasmic protein with a potential role in iron transport

Cartron, M. L., Mitchell, S., Woodhall, M. R., Andrews, S. C. and Watson, K. A. (2007) Preliminary X-ray diffraction analysis of YcdB from Escherichia coli: a novel haem-containing and Tat-secreted periplasmic protein with a potential role in iron transport. Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 63. pp. 37-41. ISSN 1744-3091

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To link to this article DOI: 10.1107/s174430910604509x

Abstract/Summary

YcdB is a periplasmic haem-containing protein from Escherichia coli that has a potential role in iron transport. It is currently the only reported haem-containing Tat-secreted substrate. Here, the overexpression, purification, crystallization and structure determination at 2.0 angstrom resolution are reported for the apo form of the protein. The apo-YcdB structure resembles those of members of the haem-dependent peroxidase family and thus confirms that YcdB is also a member of this family. Haem-soaking experiments with preformed apo-YcdB crystals have been optimized to successfully generate haem-containing YcdB crystals that diffract to 2.9 angstrom. Completion of model building and structure refinement are under way.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences
Interdisciplinary centres and themes > Institute for Cardiovascular and Metabolic Research (ICMR)
Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
Faculty of Life Sciences > School of Biological Sciences
ID Code:9961
Uncontrolled Keywords:MOLECULAR REPLACEMENT, BACILLUS-SUBTILIS, FUR REGULON, GENES, HOMEOSTASIS, PEROXIDASE, EXPRESSION

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