4V4E

Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici complexed with inhibitor 1,2,4,5-tetrahydroxy-benzene

This is a non-PDB format compatible entry.

Summary for 4V4E

• Entry DOI: 10.2210/pdb4v4e/pdb
• Related: 1TI2 1TI4 1VLD 1VLE
• Descriptor: Pyrogallol hydroxytransferase large subunit, Pyrogallol hydroxytransferase small subunit, CALCIUM ION, ... (8 entities in total)
• Functional Keywords: molybdenum binding enzyme, mgd-cofactors, dmso-reductase family, 4fe-4s-cluster, complex with inhibitor 1, 2, 4, 5-tetrahydroxy benzene, oxidoreductase
• Biological source: Pelobacter acidigallici; More
• Total number of polymer chains: 24
• Total formula weight: 1601922.73

Authors

Messerschmidt, A.,Niessen, H.,Abt, D.,Einsle, O.,Schink, B.,Kroneck, P.M.H. (deposition date: 2004-06-02, release date: 2014-07-09, Last modification date: 2023-09-20)

Primary citation

Messerschmidt, A.,Niessen, H.,Abt, D.,Einsle, O.,Schink, B.,Kroneck, P.M.H.
Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols
PROC.NATL.ACAD.SCI.USA, 101:11571-11576, 2004

PubMed 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.

PubMed: 15284442
DOI: 10.1073/pnas.0404378101

Experimental method

X-RAY DIFFRACTION (2 Å)