1CL1

CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI

1CL1 の概要

• エントリーDOI: 10.2210/pdb1cl1/pdb
• 分子名称: CYSTATHIONINE BETA-LYASE, BICARBONATE ION (3 entities in total)
• 機能のキーワード: plp-dependent enzymes, methionine biosynthesis, c-s beta lyase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P06721
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87100.81

構造登録者

Clausen, T.,Huber, R.,Messerschmidt, A. (登録日: 1997-09-02, 公開日: 1998-09-09, 最終更新日: 2023-11-15)

主引用文献

Clausen, T.,Huber, R.,Laber, B.,Pohlenz, H.D.,Messerschmidt, A.
Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A.
J.Mol.Biol., 262:202-224, 1996

PubMed Abstract: Cystathionine beta-lyase (CBL) is a member of the gamma-family of PLP-dependent enzymes, that cleaves C beta-S bonds of a broad variety of substrates. The crystal structure of CBL from E. coli has been solved using MIR phases in combination with density modification. The structure has been refined to an R-factor of 15.2% at 1.83 A resolution using synchroton radiation diffraction data. The asymmetric unit of the crystal cell (space group C222(1)) contains two monomers related by 2-fold symmetry. A homotetramer with 222 symmetry is built up by crystallographic and non-crystallographic symmetry. Each monomer of CBL can be described in terms of three spatially and functionally different domains. The N-terminal domain (residues 1 to 60) consists of three alpha-helices and one beta-strand. It contributes to tetramer formation and is part of the active site of the adjacent subunit. The second domain (residues 61 to 256) harbors PLP and has an alpha/beta-structure with a seven-stranded beta-sheet as the central part. The remaining C-terminal domain (residues 257 to 395), connected by a long alpha-helix to the PLP-binding domain, consists of four helices packed on the solvent-accessible side of an antiparallel four-stranded beta-sheet. The fold of the C-terminal and the PLP-binding domain and the location of the active site are similar to aminotransferases. Most of the residues in the active site are strongly conserved among the enzymes of the transsulfuration pathway. Additionally, CBL is homologous to the mal gamma gene product indicating an evolutionary relationship between alpha and gamma-family of PLP-dependent enzymes. The structure of the beta, beta, beta-trifluoroalanine inactivated CBL has been refined at 2.3 A resolution to an R-factor of 16.2%. It suggests that Lys210, the PLP-binding residue, mediates the proton transfer between C alpha and S gamma.

PubMed: 8831789
DOI: 10.1006/jmbi.1996.0508

実験手法

X-RAY DIFFRACTION (1.83 Å)