2bf3

From Proteopedia

Revision as of 10:40, 30 October 2007

CRYSTAL STRUCTURE OF A TOLUENE 4-MONOOXYGENASE CATALYTIC EFFECTOR PROTEIN VARIANT MISSING TEN N-TERMINAL RESIDUES (DELTA-N10 T4MOD)

Overview

Toluene 4-monooxygenase (T4MO) is a four-component complex that catalyzes, the regiospecific, NADH-dependent hydroxylation of toluene to yield, p-cresol. The catalytic effector (T4moD) of this complex is a 102-residue, protein devoid of metals or organic cofactors. It forms a complex with the, diiron hydroxylase component (T4moH) that influences both the kinetics and, regiospecificity of catalysis. Here, we report crystal structures for, native T4moD and two engineered variants with either four (DeltaN4-) or 10, (DeltaN10-) residues removed from the N-terminal at 2.1-, 1.7-, and 1.9-A, resolution, respectively. The crystal structures have C-alpha, root-mean-squared differences of less than 0.8 A for the central core, consisting of residues 11-98, showing that alterations of the ... [(full description)]

About this Structure

2BF3 is a [Protein complex] structure of sequences from [Pseudomonas mendocina] with HTO as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structures and functional studies of T4moD, the toluene 4-monooxygenase catalytic effector protein., Lountos GT, Mitchell KH, Studts JM, Fox BG, Orville AM, Biochemistry. 2005 May 17;44(19):7131-42. PMID:15882052

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