PDBsum entry 1ti2

Oxidoreductase

PDB id: 1ti2

Contents

Protein chains

(+ 0 more) 875 a.a. *

(+ 0 more) 274 a.a. *

Ligands

ACT ×6

MGD ×12

SF4 ×18

Metals

4MO ×6

_CA ×12

Waters ×5097

* Residue conservation analysis

Obsolete entry

PDB id:

1ti2

Name:

Oxidoreductase

Title:

Crystal structure of pyrogallol-phloroglucinol transhydroxylase from pelobacter acidigallici

Structure:

Pyrogallol hydroxytransferase large subunit. Chain: a, c, e, g, i, k. Synonym: transhydroxylase alpha subunit. Pyrogallol hydroxytransferase small subunit. Chain: b, d, f, h, j, l. Synonym: transhydroxylase beta subunit. Ec: 1.97.1.2

Source:

Pelobacter acidigallici. Organism_taxid: 35816. Strain: magal 2(dsm 2377). Strain: magal 2(dsm 2377)

Biol. unit:

Dodecamer (from PQS)

Resolution:

2.35Å R-factor: 0.198 R-free: 0.254

Authors:

A.Messerschmidt,H.Niessen,D.Abt,O.Einsle,B.Schink,P.M.H.Kroneck

Key ref:

A.Messerschmidt et al. (2004). Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols. Proc Natl Acad Sci U S A, 101, 11571-11576. PubMed id: 15284442 DOI: 10.1073/pnas.0404378101

Date:

02-Jun-04 Release date: 10-Aug-04

Protein chains

P80563  (PGTL_PELAC) -  Pyrogallol hydroxytransferase large subunit from Pelobacter acidigallici

Seq: 875 a.a.

Struc: 875 a.a.

Protein chains

P80564  (PGTS_PELAC) -  Pyrogallol hydroxytransferase small subunit from Pelobacter acidigallici

Seq: 274 a.a.

Struc: 274 a.a.

Enzyme reactions

• Enzyme class: Chains A, C, E, G, I, K: E.C.1.97.1.2 - pyrogallol hydroxytransferase.
• Reaction: 1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = 1,2,3,5- tetrahydroxybenzene + 1,3,5-trihydroxybenzene
• Cofactor: Mo cation

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1073/pnas.0404378101

Proc Natl Acad Sci U S A 101:11571-11576 (2004)

PubMed id: 15284442

Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols.

A.Messerschmidt, H.Niessen, D.Abt, O.Einsle, B.Schink, P.M.Kroneck.

ABSTRACT

The Mo enzyme transhydroxylase from the anaerobic microorganism Pelobacter acidigallici catalyzes the conversion of pyrogallol to phloroglucinol. Such trihydroxybenzenes and their derivatives represent important building blocks of plant polymers. None of the transferred hydroxyl groups originates from water during transhydroxylation; instead a cosubstrate, such as 1,2,3,5-tetrahydroxybenzene, is used in a reaction without apparent electron transfer. Here, we report on the crystal structure of the enzyme in the reduced Mo(IV) state, which we solved by single anomalous-diffraction technique. It represents the largest structure (1,149 amino acid residues per molecule, 12 independent molecules per unit cell), which has been solved so far by single anomalous-diffraction technique. Tranhydroxylase is a heterodimer, with the active Mo-molybdopterin guanine dinucleotide (MGD)(2) site in the alpha-subunit, and three [4Fe-4S] centers in the beta-subunit. The latter subunit carries a seven-stranded, mainly antiparallel beta-barrel domain. We propose a scheme for the transhydroxylation reaction based on 3D structures of complexes of the enzyme with various polyphenols serving either as substrate or inhibitor.

Selected figure(s)

Figure 1.
Fig. 1. Overall structure of TH. The -subunit domains I-IV are shown in magenta, blue, red, and cream, respectively. The -subunit domains I and II are shown in orange and pink, respectively, and domain III is shown in green. The Mo and MGD cofactors are shown as ball-and-stick models, and the three [4Fe--4S] clusters are shown as red (Fe) and yellow (S) spheres. The figure was made with BOBSCRIPT (31) and RASTER3D (32).

Figure 2.
Fig. 2. Solid-surface-electrostatic potential representation of TH displaying the access channel for substrate and cosubstrate. The electrostatic surface potentials are contoured from -10 (red) to 10 K[B]T/e (blue). The figure was made with GRASP (34) and RASTER3D (32).

Figures were selected by an automated process.