1PYA

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

Summary for 1PYA

• Entry DOI: 10.2210/pdb1pya/pdb
• Descriptor: PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE (L-HISTIDINE CARBOXYLASE) (3 entities in total)
• Functional Keywords: carboxy-lyase
• Biological source: Lactobacillus sp. 30A; More
• Total number of polymer chains: 6
• Total formula weight: 102408.62

Authors

Gallagher, T.,Rozwarski, D.A.,Ernst, S.R.,Hackert, M.L. (deposition date: 1992-12-18, release date: 1994-01-31, Last modification date: 2023-11-15)

Primary citation

Gallagher, T.,Rozwarski, D.A.,Ernst, S.R.,Hackert, M.L.
Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a.
J.Mol.Biol., 230:516-528, 1993

PubMed 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.

PubMed: 8464063
DOI: 10.1006/jmbi.1993.1168

Experimental method

X-RAY DIFFRACTION (2.5 Å)