Crystal structure of a DyP-type peroxidase 5G5 variant from Bacillus subtilis

Loops around the Heme Pocket Have a Critical Role in the Function and Stability of Bs DyP from Bacillus subtilis .

MSDEQKKPEQIHRRDILKWGAMAGAAVAIGASGLGGLAPLVQTAAKPSKKDEKEEEQIVPFYGKHQAGITTAHQTYVYFA
ALDVTAKDKSDIITLFRNWTSLTQMLTSGKKMSAEQRNQYLPPQDTGESADLSPSNLTVTFGFGPGFFEKDGKDRFGLKS
KKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFLSGGKNGETPRNLFGFKD
GTGNQSTKDDTLMNSIVWIQSGEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSSGAPFGQKKETDPVELNQ
IPSNPHVSLVKSTGKQILRRAFSYTEGLDPKTGYMDAGLLFISFQKNPDNQFIPMLKALSAKDALNEYTQTIGSALYACP
GGCKKGEYIAQRLLES

0.1 M Tris-HCl pH 8.5, 25% (w/v) PEG 4K, 0.2 M magnesium chloride

H2020 Marie Curie Actions of the European Commission

Foundation for Science and Technology (FCT)

Dye-decolorizing Peroxidase, Bacillus subtilis, Directed evolution, high-throughput screening, phenolic compounds, OXIDOREDUCTASE

(chain A and (resid 56 through 111 or resid 117 through 414))

(chain C and (resid 56 through 111 or resid 117 through 414))

(chain D and (resid 56 through 308 or resid 322 through 414))

MSDEQKKPEQIHRRDILKWGAMAGAAVAIGASGLGGLAPLVQTAAKPSKKDEKEEEQIVPFYGKHQAGITTAHQTYVYFA
ALDVTAKDKSDIITLFRNWTSLTQMLTSGKKMSAEQRNQYLPPQDTGESADLSPSNLTVTFGFGPGFFEKDGKDRFGLKS
KKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFLSGGKNGETPRNLFGFKD
GTGNQSTKDDTLMNSIVWIQSGEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSSGAPFGQKKETDPVKLNQ
IPSNSHVSLAKSTGKQILRRAFSYTEGLDPKTGYMDAGLLFISFQKNPDNQFIPMLKALSAKDALNEYTQTIGSALYACP
GGCKKGEYIAQRLLES