8JUI
Crystal structures of Cystathionine beta lyase from Bacillus cereus ATCC 14579
Summary for 8JUI
| Entry DOI | 10.2210/pdb8jui/pdb |
| Descriptor | Cystathionine beta-lyase (2 entities in total) |
| Functional Keywords | plp dependent enzyme, lyase |
| Biological source | Bacillus cereus ATCC 14579 |
| Total number of polymer chains | 1 |
| Total formula weight | 43645.18 |
| Authors | Yu, H.,Kim, K.-J. (deposition date: 2023-06-26, release date: 2024-07-03, Last modification date: 2024-12-18) |
| Primary citation | 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 Cited by 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: 39644606DOI: 10.1016/j.bbrc.2024.151122 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
