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.
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 A 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 A. Completion of model building and structure refinement are under way.
Cartron
Michaël L
ML
School of Biological Sciences, University of Reading, England.
Mitchell
Sue A
SA
Woodhall
Mark R
MR
Andrews
Simon C
SC
Watson
Kimberly A
KA
D001692:Biological Transport / Q000502:physiology; D029968:Escherichia coli Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006420:Hemeproteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D007501:Iron / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D033903:Periplasmic Proteins / Q000737:chemistry* / Q000378:metabolism; D014961:X-Ray Diffraction
D029968:Escherichia coli Proteins; D006420:Hemeproteins; D026901:Membrane Transport Proteins; D033903:Periplasmic Proteins; C511803:YcdB protein, E coli; C408585:twin-arginine translocase complex, E coli; D007501:Iron