4V4D
Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici complexed with pyrogallol
This is a non-PDB format compatible entry.
Summary for 4V4D
| Entry DOI | 10.2210/pdb4v4d/pdb |
| Related | 1TI2 1TI6 1VLD 1VLF |
| 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 substrate pyrogallol, oxidoreductase |
| Biological source | Pelobacter acidigallici More |
| Total number of polymer chains | 24 |
| Total formula weight | 1601690.67 |
| 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 Cited by 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: 15284442DOI: 10.1073/pnas.0404378101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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