3G0T
Crystal structure of putative aspartate aminotransferase (NP_905498.1) from Porphyromonas gingivalis W83 at 1.75 A resolution
Summary for 3G0T
| Entry DOI | 10.2210/pdb3g0t/pdb |
| Descriptor | Putative aminotransferase, SODIUM ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | np_905498.1, putative aspartate aminotransferase, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, aminotransferase, transferase |
| Biological source | Porphyromonas gingivalis |
| Total number of polymer chains | 2 |
| Total formula weight | 102770.83 |
| Authors | Joint Center for Structural Genomics (JCSG) (deposition date: 2009-01-28, release date: 2009-02-10, Last modification date: 2023-02-01) |
| Primary citation | Fleischman, N.M.,Das, D.,Kumar, A.,Xu, Q.,Chiu, H.J.,Jaroszewski, L.,Knuth, M.W.,Klock, H.E.,Miller, M.D.,Elsliger, M.A.,Godzik, A.,Lesley, S.A.,Deacon, A.M.,Wilson, I.A.,Toney, M.D. Molecular characterization of novel pyridoxal-5'-phosphate-dependent enzymes from the human microbiome. Protein Sci., 23:1060-1076, 2014 Cited by PubMed Abstract: Pyridoxal-5'-phosphate or PLP, the active form of vitamin B6, is a highly versatile cofactor that participates in a large number of mechanistically diverse enzymatic reactions in basic metabolism. PLP-dependent enzymes account for ∼1.5% of most prokaryotic genomes and are estimated to be involved in ∼4% of all catalytic reactions, making this an important class of enzymes. Here, we structurally and functionally characterize three novel PLP-dependent enzymes from bacteria in the human microbiome: two are from Eubacterium rectale, a dominant, nonpathogenic, fecal, Gram-positive bacteria, and the third is from Porphyromonas gingivalis, which plays a major role in human periodontal disease. All adopt the Type I PLP-dependent enzyme fold and structure-guided biochemical analysis enabled functional assignments as tryptophan, aromatic, and probable phosphoserine aminotransferases. PubMed: 24888348DOI: 10.1002/pro.2493 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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