BRASSICA NAPUS ENOYL ACP REDUCTASE/NADH BINARY COMPLEX AT PH 8.0 AND ROOM TEMPERATURE

Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase.

Crystallization of the Nadh-Specific Enoyl Acyl Carrier Protein Reductase from Brassica Napus

SESSESKASSGLPIDLRGKRAFIAGIADDNGYGWAVAKSLAAAGAEILVGTWVPALNIFETSLRRGKFDQSRVLPDGSLM
EIKKVYPLDAVFDNPEDVPEDVKANKRYAGSSNWTVQEAAECVRQDFGSIDILVHSLANGPEVSKPLLETSRKGYLAAIS
ASSYSFVSLLSHFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALESDTRVLAFEAGRKQNIRVNTISAGPLGSRA
AKAIGFIDTMIEYSYNNAPIQKTLTADEVGNAAAFLVSPLASAITGATIYVDNGLNSMGVALDSPVFKDLDK

THE STRUCTURE OF THE BINARY COMPLEX WITH NADH WAS DETERMINED BY DIFFERENCE FOURIER ANALYSIS USING DATA FROM CRYSTALS GROWN WITH NAD WHICH WERE THEN SOAKED IN NADH. THE ELECTRON DENSITY IS CLEARLY INTERPRETABLE FOR THE ENTIRE NADH COFACTOR INCLUDING THE NICOTINAMIDE MOIETY. THE ONLY SIGNIFICANT DIFFERENCE FROM THE STRUCTURE WITH NAD BOUND IS THE MOVEMENT OF THE SIDE CHAIN OF TYR 32 (WHICH WOULD OTHERWISE HAVE OCCUPIED SOME OF THE BINDING POCKET FOR THE NICOTINAMIDE RING) AND SMALL CHANGES ARE NOTED IN THE POSITIONS OF THE MAIN CHAIN FOR RESIDUES GLY 234, PRO 235, LEU 236, AND GLY 237.

OXIDOREDUCTASE, PLANT LIPID BIOSYNTHESIS

MAATAAASSLQMATTRPSISAASSKARTYVVGANPRNAYKIACTPHLSNLGCLRNDSALPASKKSFSFSTKAMSESSESK
ASSGLPIDLRGKRAFIAGIADDNGYGWAVAKSLAAAGAEILVGTWVPALNIFETSLRRGKFDQSRVLPDGSLMEIKKVYP
LDAVFDNPEDVPEDVKANKRYAGSSNWTVQEAAECVRQDFGSIDILVHSLANGPEVSKPLLETSRKGYLAAISASSYSFV
SLLSHFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALESDTRVLAFEAGRKQNIRVNTISAGPLGSRAAKAIGFI
DTMIEYSYNNAPIQKTLTADEVGNAAAFLVSPLASAITGATIYVDNGLNSMGVALDSPVFKDLNK