1ZPD

PYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILIS

Summary for 1ZPD

• Entry DOI: 10.2210/pdb1zpd/pdb
• Descriptor: PYRUVATE DECARBOXYLASE, MAGNESIUM ION, MONO-{4-[(4-AMINO-2-METHYL-PYRIMIDIN-5-YLMETHYL)-AMINO]-2-HYDROXY-3-MERCAPTO-PENT-3-ENYL-PHOSPHONO} ESTER, ... (5 entities in total)
• Functional Keywords: alcohol fermentation, thiamin diphosphate, decarboxylase
• Biological source: Zymomonas mobilis
• Total number of polymer chains: 4
• Total formula weight: 246416.08

Authors

Lu, G.,Dobritzsch, D.,Schneider, G. (deposition date: 1998-04-17, release date: 1999-02-02, Last modification date: 2024-05-22)

Primary citation

Dobritzsch, D.,Konig, S.,Schneider, G.,Lu, G.
High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases.
J.Biol.Chem., 273:20196-20204, 1998

PubMed Abstract: The crystal structure of tetrameric pyruvate decarboxylase from Zymomonas mobilis has been determined at 1.9 A resolution and refined to a crystallographic R-factor of 16.2% and Rfree of 19.7%. The subunit consists of three domains, all of the alpha/beta type. Two of the subunits form a tight dimer with an extensive interface area. The thiamin diphosphate binding site is located at the subunit-subunit interface, and the cofactor, bound in the V conformation, interacts with residues from the N-terminal domain of one subunit and the C-terminal domain of the second subunit. The 2-fold symmetry generates the second thiamin diphosphate binding site in the dimer. Two of the dimers form a tightly packed tetramer with pseudo 222 symmetry. The interface area between the dimers is much larger in pyruvate decarboxylase from Z. mobilis than in the yeast enzyme, and structural differences in these parts result in a completely different packing of the subunits in the two enzymes. In contrast to other pyruvate decarboxylases, the enzyme from Z. mobilis is not subject to allosteric activation by the substrate. The tight packing of the dimers in the tetramer prevents large rearrangements in the quaternary structure as seen in the yeast enzyme and locks the enzyme in an activated conformation. The architecture of the cofactor binding site and the active site is similar in the two enzymes. However, the x-ray analysis reveals subtle but significant structural differences in the active site that might be responsible for variations in the biochemical properties in these enzymes.

PubMed: 9685367
DOI: 10.1074/jbc.273.32.20196

Experimental method

X-RAY DIFFRACTION (1.86 Å)