1w54

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spinqualitylabelsall models 1w54, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STEPWISE INTRODUCTION OF A ZINC BINDING SITE INTO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA (MUTATION D139C)

Overview

Metal ions are indispensable cofactors for chemical catalysis by a, plethora of enzymes. Porphobilinogen synthases (PBGSs), which catalyse the, second step of tetrapyrrole biosynthesis, are grouped according to their, dependence on Zn(2+). Using site-directed mutagenesis, we embarked on, transforming Zn(2+)-independent Pseudomonas aeruginosa PBGS into a, Zn(2+)-dependent enzyme. Nine PBGS variants were generated by, permutationally introducing three cysteine residues and a further two, residues into the active site of the enzyme to match the homologous, Zn(2+)-containing PBGS from Escherichia coli. Crystal structures of seven, enzyme variants were solved to elucidate the nature of Zn(2+) coordination, at high resolution. The three single-cysteine variants were invariably, found to be ... [(full description)]

About this Structure

1W54 is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with K, MG, ZN and FMT as [ligands]. Active as [[1]], with EC number [4.2.1.24]. Full crystallographic information is available from [OCA].

Reference

Tracking the evolution of porphobilinogen synthase metal dependence in vitro., Frere F, Reents H, Schubert WD, Heinz DW, Jahn D, J Mol Biol. 2005 Feb 4;345(5):1059-70. Epub 2004 Dec 21. PMID:15644204

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