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. 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 Sat May 3 08:35:24 2008
