title: NMR assignment of the periplasmic oxidoreductase DsbH from Chlamydia.
abstract: Chlamydia use a complex of outer envelope proteins, which are highly cross-linked by disulfide bonds, to protect their infectious developmental form from lysis. Reported herein are the NMR chemical shift assignments of DsbH, a novel disulfide oxidoreductase from Chlamydia.
authors.affiliation: Department of Biochemistry & Molecular Biology, Zilkha Neurogenetic Institute, University of Southern California, Los Angeles, 90033, USA.
authors.forename: Kuo-Chan
authors.initials: KC
authors.lastname: Hung
authors.forename: Thien-Thi
authors.initials: TT
authors.lastname: Mac
authors.forename: Tobias S
authors.initials: TS
authors.lastname: Ulmer
mesh_terms: D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D016993:Chlamydophila pneumoniae / Q000201:enzymology*; D004220:Disulfides / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D010088:Oxidoreductases / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011522:Protons
chemical_list: D002247:Carbon Isotopes; D004220:Disulfides; D005656:Fungal Proteins; D009587:Nitrogen Isotopes; D011522:Protons; D010088:Oxidoreductases