1pya

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spinqualitylabelsall models 1pya, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE FROM LACTOBACILLUS 30A

Overview

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.

About this Structure

1PYA is a Protein complex structure of sequences from Lactobacillus sp.. Active as Histidine decarboxylase, with EC number 4.1.1.22 Full crystallographic information is available from OCA.

Reference

Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a., Gallagher T, Rozwarski DA, Ernst SR, Hackert ML, J Mol Biol. 1993 Mar 20;230(2):516-28. PMID:8464063

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