NMR assignment of the periplasmic oxidoreductase DsbH from Chlamydia.
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.
Hung
Kuo-Chan
KC
Department of Biochemistry & Molecular Biology, Zilkha Neurogenetic Institute, University of Southern California, Los Angeles, 90033, USA.
Mac
Thien-Thi
TT
Ulmer
Tobias S
TS
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
D002247:Carbon Isotopes; D004220:Disulfides; D005656:Fungal Proteins; D009587:Nitrogen Isotopes; D011522:Protons; D010088:Oxidoreductases