1gzg

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spinqualitylabelsall models 1gzg, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

COMPLEX OF A MG2-DEPENDENT PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA (MUTANT D139N) WITH 5-FLUOROLEVULINIC ACID

Overview

All natural tetrapyrroles, including hemes, chlorophylls and vitamin B12, share porphobilinogen (PBG) as a common precursor. Porphobilinogen, synthase (PBGS) synthesizes PBG through the asymmetric condensation of two, molecules of aminolevulinic acid (ALA). Crystal structures of PBGS from, various sources confirm the presence of two distinct binding sites for, each ALA molecule, termed A and P. We have solved the structure of the, active-site variant D139N of the Mg2+-dependent PBGS from Pseudomonas, aeruginosa in complex with the inhibitor 5-fluorolevulinic acid at high, resolution. Uniquely, full occupancy of both substrate binding sites each, by a single substrate-like molecule was observed. Both inhibitor molecules, are covalently bound to two conserved, active-site lysine residues, ... [(full description)]

About this Structure

1GZG is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with MG, NA, SO4, K and LAF as [ligands]. Active as [Porphobilinogen synthase], with EC number [4.2.1.24]. Structure known Active Site: LA1. Full crystallographic information is available from [OCA].

Reference

Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism., Frere F, Schubert WD, Stauffer F, Frankenberg N, Neier R, Jahn D, Heinz DW, J Mol Biol. 2002 Jul 5;320(2):237-47. PMID:12079382

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