5EUJ

PYRUVATE DECARBOXYLASE FROM ZYMOBACTER PALMAE

This is a non-PDB format compatible entry.

Summary for 5EUJ

• Entry DOI: 10.2210/pdb5euj/pdb
• Descriptor: Pyruvate decarboxylase, MAGNESIUM ION, THIAMINE DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: pyruvate decarboxylase, lyase
• Biological source: Zymobacter palmae
• Total number of polymer chains: 24
• Total formula weight: 1496179.58

Authors

Buddrus, L.,Crennell, S.J.,Leak, D.J.,Danson, M.J.,Andrews, E.S.V.,Arcus, V.L. (deposition date: 2015-11-18, release date: 2016-09-14, Last modification date: 2024-01-10)

Primary citation

Buddrus, L.,Andrews, E.S.,Leak, D.J.,Danson, M.J.,Arcus, V.L.,Crennell, S.J.
Crystal structure of pyruvate decarboxylase from Zymobacter palmae.
Acta Crystallogr.,Sect.F, 72:700-706, 2016

PubMed Abstract: Pyruvate decarboxylase (PDC; EC 4.1.1.1) is a thiamine pyrophosphate- and Mg(2+) ion-dependent enzyme that catalyses the non-oxidative decarboxylation of pyruvate to acetaldehyde and carbon dioxide. It is rare in bacteria, but is a key enzyme in homofermentative metabolism, where ethanol is the major product. Here, the previously unreported crystal structure of the bacterial pyruvate decarboxylase from Zymobacter palmae is presented. The crystals were shown to diffract to 2.15 Å resolution. They belonged to space group P21, with unit-cell parameters a = 204.56, b = 177.39, c = 244.55 Å and Rr.i.m. = 0.175 (0.714 in the highest resolution bin). The structure was solved by molecular replacement using PDB entry 2vbi as a model and the final R values were Rwork = 0.186 (0.271 in the highest resolution bin) and Rfree = 0.220 (0.300 in the highest resolution bin). Each of the six tetramers is a dimer of dimers, with each monomer sharing its thiamine pyrophosphate across the dimer interface, and some contain ethylene glycol mimicking the substrate pyruvate in the active site. Comparison with other bacterial PDCs shows a correlation of higher thermostability with greater tetramer interface area and number of interactions.

PubMed: 27599861
DOI: 10.1107/S2053230X16012012

Experimental method

X-RAY DIFFRACTION (2.15 Å)