1sdw
From Proteopedia
|
Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase with bound peptide and dioxygen
Overview
Copper active sites play a major role in enzymatic activation of dioxygen., We trapped the copper-dioxygen complex in the enzyme, peptidylglycine-alphahydroxylating monooxygenase (PHM) by freezing protein, crystals that had been soaked with a slow substrate and ascorbate in the, presence of oxygen. The x-ray crystal structure of this precatalytic, complex, determined to 1.85-angstrom resolution, shows that oxygen binds, to one of the coppers in the enzyme with an end-on geometry. Given this, structure, it is likely that dioxygen is directly involved in the electron, transfer and hydrogen abstraction steps of the PHM reaction. These, insights may apply to other copper oxygen-activating enzymes, such as, dopamine beta-monooxygenase, and to the design of biomimetic complexes.
About this Structure
1SDW is a Single protein structure of sequence from Rattus norvegicus with CU, NI, OXY, IYT and GOL as ligands. Active as Peptidylglycine monooxygenase, with EC number 1.14.17.3 Full crystallographic information is available from OCA.
Reference
Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex., Prigge ST, Eipper BA, Mains RE, Amzel LM, Science. 2004 May 7;304(5672):864-7. PMID:15131304
Page seeded by OCA on Wed Nov 21 02:18:24 2007
Categories: Peptidylglycine monooxygenase | Rattus norvegicus | Single protein | Amzel, L.M. | Eipper, B.A. | Mains, R.E. | Prigge, S.T. | CU | GOL | IYT | NI | OXY | Beta jelly-roll
