2O0T
The three dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation
Summary for 2O0T
| Entry DOI | 10.2210/pdb2o0t/pdb |
| Related | 1HKV 1HKW |
| Descriptor | Diaminopimelate decarboxylase, SULFATE ION (3 entities in total) |
| Functional Keywords | plp binding enzyme, decarboxylase, lysine biosynthesis, structural genomics, tb structural genomics consortium, tbsgc, lyase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 4 |
| Total formula weight | 199805.39 |
| Authors | Weyand, S.,Kefala, G.,Weiss, M.S.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2006-11-28, release date: 2007-02-13, Last modification date: 2023-11-15) |
| Primary citation | Weyand, S.,Kefala, G.,Svergun, D.I.,Weiss, M.S. The three-dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation. J Struct Funct Genomics, 10:209-217, 2009 Cited by PubMed 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 A. The monoclinic crystals contain one tetramer exhibiting D(2)-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. PubMed: 19543810DOI: 10.1007/s10969-009-9065-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.33 Å) |
Structure validation
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