title: The crystal and solution structure of YdiE from Escherichia coli.
abstract: Iron-containing porphyrins are essential for all life as electron carriers. Since iron is poorly available in an oxidizing environment, bacterial growth may be restricted by iron limitation, and this has led to the evolution of a huge variety of iron-uptake systems. Among pathogens, iron scavenging from the haemoglobin of an animal host is a common means of acquiring sufficient iron for growth. The Isd system of Staphylococcus aureus is a well studied example; the bacterium devotes considerable resources to the construction of surface proteins that deftly remove haem from haemoglobin and pass it along a chain of related proteins, eventually delivering the haem to the cytoplasm, where it can be utilized or degraded. All organisms, however, must deal with haem and related molecules, which are by their nature hydrophobic and prone to precipitate, and which tend to promote the formation of reactive oxygen species. Chaperones are an obvious solution to the problem of maintaining a pool of haem for insertion into cytochromes without allowing naked haem to cause damage. YdiE is a very small protein from Escherichia coli of only 63 residues which may play a role in haem trafficking. Here, NMR analysis and the crystal structure of the protein to high resolution are reported.
authors.affiliation: Drug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
authors.forename: Kaoru
authors.initials: K
authors.lastname: Nishimura
authors.affiliation: Drug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
authors.forename: Christine
authors.initials: C
authors.lastname: Addy
authors.affiliation: Structural Bioinformatics Team, Division of Structural and Synthetic Biology, Center for Life Science Technologies, RIKEN, 1-7-22 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
authors.forename: Rojan
authors.initials: R
authors.lastname: Shrestha
authors.affiliation: Structural Bioinformatics Team, Division of Structural and Synthetic Biology, Center for Life Science Technologies, RIKEN, 1-7-22 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
authors.forename: Arnout R D
authors.initials: AR
authors.lastname: Voet
authors.affiliation: Structural Bioinformatics Team, Division of Structural and Synthetic Biology, Center for Life Science Technologies, RIKEN, 1-7-22 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
authors.forename: Kam Y J
authors.initials: KY
authors.lastname: Zhang
authors.affiliation: Department of Chemistry, Tokyo Metropolitan University, 1-1 Minami-Osawa, Hachioji, Tokyo 192-0397, Japan.
authors.forename: Yutaka
authors.initials: Y
authors.lastname: Ito
authors.affiliation: Drug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
authors.forename: Jeremy R H
authors.initials: JR
authors.lastname: Tame
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000302:isolation & purification; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012996:Solutions / Q000737:chemistry
chemical_list: D029968:Escherichia coli Proteins; D012996:Solutions
keywords: Escherichia coli; YdiE; dimer; haem; intrinsic disorder; iron transport; small protein