8JUI

Crystal structures of Cystathionine beta lyase from Bacillus cereus ATCC 14579

8JUI の概要

• エントリーDOI: 10.2210/pdb8jui/pdb
• 分子名称: Cystathionine beta-lyase (2 entities in total)
• 機能のキーワード: plp dependent enzyme, lyase
• 由来する生物種: Bacillus cereus ATCC 14579
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43645.18

構造登録者

Yu, H.,Kim, K.-J. (登録日: 2023-06-26, 公開日: 2024-07-03, 最終更新日: 2024-12-18)

主引用文献

Lee, S.H.,Yu, H.,Hong, J.,Seok, J.,Kim, K.J.
Crystal structures of cystathionine beta-lyase and cystathionine beta-lyase like protein from Bacillus cereus ATCC 14579.
Biochem.Biophys.Res.Commun., 742:151122-151122, 2024

PubMed Abstract: Cystathionine β-lyase (CBL) and cystathionine β-lyase-like protein (CBLP) are key PLP-dependent enzymes involved in methionine biosynthesis. In Bacillus cereus ATCC 14579 CBL (BcCBL) and CBLP (BcCBLP) catalyze the conversion of cystathionine to homocysteine and pyruvate. In this study, we found that both BcCBL and BcCBLP effectively catalyze cystathionine cleavage, with BcCBLP exhibiting a higher catalytic efficiency (kcat) and low substrate affinity (K). We determined their crystal structures in complex with pyridoxal phosphate (PLP). BcCBL, forming a tetramer, aligns with typical CBLs in sulfur amino acid metabolism, while BcCBLP, forming a dimer, resembles the bifunctional MalY enzyme from Escherichia coli, indicating potential additional regulatory roles. These structural and functional insights highlight the distinct roles of BcCBL and BcCBLP in cellular metabolism. This study provides valuable insights into the structural diversity and potential functions of these enzymes, contributing to the broader knowledge of PLP-dependent enzymatic mechanisms.

PubMed: 39644606
DOI: 10.1016/j.bbrc.2024.151122

実験手法

X-RAY DIFFRACTION (2.2 Å)