2c13

File:2c13.gif

spinqualitylabelsall models 2c13, resolution 2.150Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

5-HYDROXY-LEVULINIC ACID BOUND TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA

OverviewOverview

Porphobilinogen synthase catalyzes the first committed step of the, tetrapyrrole biosynthesis pathway. In an aldol-like condensation, two, molecules of 5-aminolevulinic acid (ALA) form the first pyrrole, porphobilinogen. Newly synthesized analogues of a reaction intermediate of, porphobilinogen synthase have been employed in studying the active site, and the catalytic mechanism of this early enzyme of tetrapyrrole, biosynthesis. This study combines structural and kinetic evaluation of the, inhibition potency of these inhibitors. In addition, one of the determined, protein structures provides for the first time structural evidence of a, magnesium ion in the active site. From these results, we can corroborate, an earlier postulated enzymatic mechanism that starts with formation of a, C-C bond, linking C3 of the A-side ALA to C4 of the P-side ALA through an, aldole addition. The obtained data are discussed with respect to the, current literature.

About this StructureAbout this Structure

2C13 is a Single protein structure of sequence from Pseudomonas aeruginosa with MG, CL, K, PGE and PEG as ligands. Active as Porphobilinogen synthase, with EC number 4.2.1.24 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

ReferenceReference

Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors., Frere F, Nentwich M, Gacond S, Heinz DW, Neier R, Frankenberg-Dinkel N, Biochemistry. 2006 Jul 11;45(27):8243-53. PMID:16819823

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