5XOY

Crystal structure of LysK from Thermus thermophilus in complex with Lysine

「3X3E」から置き換えられました

5XOY の概要

• エントリーDOI: 10.2210/pdb5xoy/pdb
• 分子名称: [LysW]-lysine hydrolase, LYSINE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
• 細胞内の位置: Cytoplasm : Q8VUS5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82394.79

構造登録者

Tomita, T.,Fujita, S.,Hasebe, F.,Cho, S.-H.,Yoshida, A.,Kuzuyama, T.,Nishiyama, M. (登録日: 2017-05-31, 公開日: 2017-09-13, 最終更新日: 2023-11-22)

主引用文献

Fujita, S.,Cho, S.-H.,Yoshida, A.,Hasebe, F.,Tomita, T.,Kuzuyama, T.,Nishiyama, M.
Crystal structure of LysK, an enzyme catalyzing the last step of lysine biosynthesis in Thermus thermophilus, in complex with lysine: Insight into the mechanism for recognition of the amino-group carrier protein, LysW
Biochem. Biophys. Res. Commun., 491:409-415, 2017

PubMed Abstract: LysK is an M20 peptidase family enzyme that hydrolyzes the isopeptide bond between the carrier protein LysW and lysine in order to release lysine, which is the last step of lysine biosynthesis in Thermus thermophilus. In the present study, we determined the crystal structure of LysK in complex with lysine at a resolution of 2.4 Å. The α-amino group of the bound lysine was oriented toward the catalytic center, which was composed of the residues coordinating divalent metal ions for the hydrolysis of the isopeptide bond. An 11 Å-long path was observed from the active site binding lysine to the protein surface, which may be responsible for recognizing the C-terminal extension domain of LysW with the conserved EDWGE sequence. A positively-charged surface region was detected around the exit of the path, similar to other lysine biosynthetic enzymes using LysW as the carrier protein. Mutational studies of the surface residues provided a plausible model for the electrostatic interaction with LysW.

PubMed: 28720495
DOI: 10.1016/j.bbrc.2017.07.088

実験手法

X-RAY DIFFRACTION (2.39 Å)