Mixed-valence, active form, of cytochrome c peroxidase from obligate human pathogenic bacterium Neisseria gonorrhoeae at 1.4 Angstrom resolution

Structural Characterization of Neisseria gonorrhoeae Bacterial Peroxidase-Insights into the Catalytic Cycle of Bacterial Peroxidases.

MGEDQDLLKRAQGVFQPLPTVEEMQKIRPFTEEQVKLGHQLWYEPRLSKGNTVSCNSCHNLASAGVDNMPTSQGHKGQFG
GRNSPTALNAALLGSQFWDGRAADVEEQAGGPLVNPVEMANDSQEAAAAKIAKVPEYQEMFKKAFPEDGAVSFKNITTAL
GAFERTLLTPTKWDEYLKGNVNALSEQERKGVRAFMDNGCIACHNGVNLGGTTFQKFGLVQGPYWKFIEDPKRDKGRADV
TKKTEDEFFFRVPGLRNVAKTYPYFHNGSVWELDKAVTIMGKAQLGKDIPKEDVDNIVVFLNALSGNVSESARTMPELPL
TAPMESKPD

0.1 M MES pH 6.0, 30 % 5/4 PO/OH, 2 mM CaCl2, 10 mM sodium ascorbate and 0.2 mM FMN

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY

Neisseria gonorrhoeae, bacterial peroxidase, ROS detoxification, electron transport

EDQDLLKRAQGVFQPLPTVEEMQKIRPFTEEQVKLGHQLWYEPRLSKGNTVSCNSCHNLASAGVDNMPTSQGHKGQFGGR
NSPTALNAALLGSQFWDGRAADVEEQAGGPLVNPVEMANDSQEAAAAKIAKVPEYQEMFKKAFPEDGAVSFKNITTALGA
FERTLLTPTKWDEYLKGNVNALSEQERKGVRAFMDNGCIACHNGVNLGGTTFQKFGLVQGPYWKFIEDPKRDKGRADVTK
KTEDEFFFRVPGLRNVAKTYPYFHNGSVWELDKAVTIMGKAQLGKDIPKEDVDNIVVFLNALSGNVSESARTMPELPLTA
PMESKPD