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Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a.

Gallagher T, Rozwarski DA, Ernst SR, Hackert ML
J Mol Biol 230 516-28 (1993)
Cited: 33 times
EuropePMC logo PMID: 8464063

Abstract

The crystal structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a has been refined to an R-value of 0.15 (for the 5.0 to 2.5 A resolution shell) and 0.17 (for the 10.0 to 2.5 A resolution shell). A description of the overall structure is presented, focusing on secondary structure and subunit association. The enzyme is a hexamer of alpha beta subunits. Separate alpha and beta-chains arise from an autocatalytic cleavage reaction between two serine residues, which results in the pyruvoyl cofactor. The central core of the alpha beta subunit is a beta-sandwich which consists of two face-to-face three-stranded antiparallel beta-sheets, flanked by alpha-helices on each side. The beta-sandwich creates a stable fold that allows conformational strain to be introduced across an internal cleavage region between the alpha and beta chains and places the pyruvoyl cofactor in a position for efficient electron withdrawal from the substrate. Three alpha beta subunits are related by a molecular three-fold symmetry axis to form a trimer whose interfaces have complementary surfaces and extensive molecular interactions. Each of the interfaces contains an active site and a solvent channel that leads from the active site to the exterior of the molecule. The trimers are related by a crystallographic two-fold symmetry axis to form the hexamer with an overall dumbbell shape. The interface between trimers has few molecular interactions.

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Related citations provided by authors (4)

  1. Pyruvoyl-Dependent Histidine Decarboxylase: Active Site Structure and Mechanistic Analysis. Gallagher T, Snell EE, Hackert ML J. Biol. Chem. 264 12737- (1989)
  2. Structure Determination of Histidine Decarboxylase from Lactobacillus 30A at 3.0 Angstroms Resolution. Parks EH, Ernst SR, Hamlin R, Xuong NH, Hackert ML J. Mol. Biol. 182 455- (1985)
  3. The Molecular Symmetry of Histidine Decarboxylase and Prohistidine Decarboxylase by Rotation Function Analysis. Parks EH, Clinger K, Hackert ML Acta Crystallogr., B 39 490- (1983)
  4. Crystallization and Subunit Structure of Histidine Decarboxylase from Lactobacillus 30A. Hackert ML, Meador WE, Oliver RM, Salmon JB, Rescei PA, Snell EE J. Biol. Chem. 256 687- (1981)

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