8EYS
X-ray crystal structure of salmonella typhimurium Tryptophan synthase internal aldimine at pH 5.0
Summary for 8EYS
| Entry DOI | 10.2210/pdb8eys/pdb |
| Descriptor | Tryptophan synthase alpha chain, Tryptophan synthase beta chain (3 entities in total) |
| Functional Keywords | beta-elimination, plp-dependent, lyase |
| Biological source | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) More |
| Total number of polymer chains | 2 |
| Total formula weight | 71845.79 |
| Authors | Drago, V.N.,Kovalevsky, A.Y.,Mueser, T.C. (deposition date: 2022-10-28, release date: 2024-02-14, Last modification date: 2024-05-08) |
| Primary citation | Drago, V.N.,Devos, J.M.,Blakeley, M.P.,Forsyth, V.T.,Parks, J.M.,Kovalevsky, A.,Mueser, T.C. Neutron diffraction from a microgravity-grown crystal reveals the active site hydrogens of the internal aldimine form of tryptophan synthase. Cell Rep Phys Sci, 5:-, 2024 Cited by PubMed Abstract: Pyridoxal 5'-phosphate (PLP), the biologically active form of vitamin B, is an essential cofactor in many biosynthetic pathways. The emergence of PLP-dependent enzymes as drug targets and biocatalysts, such as tryptophan synthase (TS), has underlined the demand to understand PLP-dependent catalysis and reaction specificity. The ability of neutron diffraction to resolve the positions of hydrogen atoms makes it an ideal technique to understand how the electrostatic environment and selective protonation of PLP regulates PLP-dependent activities. Facilitated by microgravity crystallization of TS with the Toledo Crystallization Box, we report the 2.1 Å joint X-ray/neutron (XN) structure of TS with PLP in the internal aldimine form. Positions of hydrogens were directly determined in both the α- and β-active sites, including PLP cofactor. The joint XN structure thus provides insight into the selective protonation of the internal aldimine and the electrostatic environment of TS necessary to understand the overall catalytic mechanism. PubMed: 38645802DOI: 10.1016/j.xcrp.2024.101827 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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