8EZC

X-ray crystal structure of salmonella typhimurium Tryptophan synthase internal aldimine

8EZC の概要

• エントリーDOI: 10.2210/pdb8ezc/pdb
• 分子名称: Tryptophan synthase alpha chain, Tryptophan synthase beta chain, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: beta-elimination, plp-dependent, lyase
• 由来する生物種: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71868.78

構造登録者

Drago, V.N.,Mueser, T.C. (登録日: 2022-10-31, 公開日: 2024-02-14, 最終更新日: 2024-05-08)

主引用文献

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

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: 38645802
DOI: 10.1016/j.xcrp.2024.101827

実験手法

X-RAY DIFFRACTION (1.6 Å)