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The three-dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation

DOI: 10.1007/s10969-009-9065-z DOI Help

Authors: Simone Weyand (EMBL Hamburg Outstation; Imperial College London; Membrane Protein Laboratory, Diamond Light Source) , Georgia Kefala (EMBL Hamburg Outstation) , Dmitri I. Svergun (EMBL Hamburg Outstation) , Manfred S. Weiss (EMBL Hamburg Outstation)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Structural And Functional Genomics , VOL 10 , PAGES 209 - 217

State: Published (Approved)
Published: June 2009

Abstract: The three-dimensional structure of the enzyme diaminopimelate decarboxylase from Mycobacterium tuberculosis has been determined in a new crystal form and refined to a resolution of 2.33 Å. The monoclinic crystals contain one tetramer exhibiting D2-symmetry in the asymmetric unit. The tetramer exhibits a donut-like structure with a hollow interior. All four active sites are accessible only from the interior of the tetrameric assembly. Small-angle X-ray scattering indicates that in solution the predominant oligomeric species of the protein is a dimer, but also that higher oligomers exist at higher protein concentrations. The observed scattering data are best explained by assuming a dimer–tetramer equilibrium with about 7% tetramers present in solution. Consequently, at the elevated protein concentrations in the crowded environment inside the cell the observed tetramer may constitute the biologically relevant functional unit of the enzyme.

Journal Keywords: X-ray crystallography; PLP-binding protein; Mycobacterium tuberculosis; LysA; Diaminopimelate decarboxylase; DAPDC; Lysine biosynthesis

Subject Areas: Biology and Bio-materials, Chemistry, Medicine


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