1biq

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spinqualitylabelsall models 1biq, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN MUTANT E238A

Overview

The R2 protein of ribonucleotide reductase catalyzes the, dioxygen-dependent one-electron oxidation of Tyr122 at a, diiron-carboxylate site. Methane monooxygenase and related hydroxylases, catalyze hydrocarbon hydroxylation at diiron sites structurally related to, the one in R2. In protein R2, the likely reaction site for dioxygen is, close to Phe208. The crystal structure of an iron ligand mutant R2, Y122F/E238A, reveals the hydroxylation of Phe208 at the meta, or epsilon-, ring position and the subsequent coordination of this residue to the, diiron site. In another mutant, F208Y, the "foreign" residue Tyr208 is, hydroxylated to Dopa. The structures of apo and diferrous F208Y presented, here suggest that Tyr208 is coordinated to the iron site of F208Y, throughout the Dopa generation ... [(full description)]

About this Structure

1BIQ is a [Protein complex] structure of sequences from [Escherichia coli] with FE2, FE, OH and HG as [ligands]. Active as [[1]], with EC number [1.17.4.1]. Full crystallographic information is available from [OCA].

Reference

Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins., Logan DT, deMare F, Persson BO, Slaby A, Sjoberg BM, Nordlund P, Biochemistry. 1998 Jul 28;37(30):10798-807. PMID:9692970

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