Document Detail


Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A.
MedLine Citation:
PMID:  8831789     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
T Clausen; R Huber; B Laber; H D Pohlenz; A Messerschmidt
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of molecular biology     Volume:  262     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  1996 Sep 
Date Detail:
Created Date:  1996-11-07     Completed Date:  1996-11-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  202-24     Citation Subset:  IM    
Affiliation:
Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried Germany.
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MeSH Terms
Descriptor/Qualifier:
Alanine / analogs & derivatives,  pharmacology
Amino Acid Sequence
Binding Sites
Crystallography, X-Ray
Enzyme Inhibitors / pharmacology
Escherichia coli / enzymology*
Lyases / antagonists & inhibitors,  chemistry*,  metabolism
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
Pyridoxal Phosphate / metabolism*
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/Enzyme Inhibitors; 17463-43-3/3,3,3-trifluoroalanine; 54-47-7/Pyridoxal Phosphate; 56-41-7/Alanine; EC 4.-/Lyases; EC 4.4.1.8/cystathionine beta-lyase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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