6PBR
Catalytic domain of E.coli dihydrolipoamide succinyltransferase in I4 space group
Summary for 6PBR
| Entry DOI | 10.2210/pdb6pbr/pdb |
| Descriptor | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, SODIUM ION (3 entities in total) |
| Functional Keywords | dihydrolipoamide succinyltransferase, 2-oxoglutarate dehydrogenase multienzyme complex, tca cycle, citric acid cycle, krebs cycle, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 6 |
| Total formula weight | 156782.46 |
| Authors | Andi, B.,Soares, A.S.,Shi, W.,Fuchs, M.R.,McSweeney, S.,Liu, Q. (deposition date: 2019-06-14, release date: 2019-06-26, Last modification date: 2023-10-11) |
| Primary citation | Andi, B.,Soares, A.S.,Shi, W.,Fuchs, M.R.,McSweeney, S.,Liu, Q. Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant. Acta Crystallogr.,Sect.F, 75:616-624, 2019 Cited by PubMed Abstract: The crystallization of amidase, the ultimate enzyme in the Trp-dependent auxin-biosynthesis pathway, from Arabidopsis thaliana was attempted using protein samples with at least 95% purity. Cube-shaped crystals that were assumed to be amidase crystals that belonged to space group I4 (unit-cell parameters a = b = 128.6, c = 249.7 Å) were obtained and diffracted to 3.0 Å resolution. Molecular replacement using structures from the PDB containing the amidase signature fold as search models was unsuccessful in yielding a convincing solution. Using the Sequence-Independent Molecular replacement Based on Available Databases (SIMBAD) program, it was discovered that the structure corresponded to dihydrolipoamide succinyltransferase from Escherichia coli (PDB entry 1c4t), which is considered to be a common crystallization contaminant protein. The structure was refined to an R of 23.0% and an R of 27.2% at 3.0 Å resolution. The structure was compared with others of the same protein deposited in the PDB. This is the first report of the structure of dihydrolipoamide succinyltransferase isolated without an expression tag and in this novel crystal form. PubMed: 31475929DOI: 10.1107/S2053230X19011488 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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