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| - | [[Image:1cl1.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1cl1| PDB=1cl1 | SCENE= }} | | {{STRUCTURE_1cl1| PDB=1cl1 | SCENE= }} |
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| - | '''CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI'''
| + | ===CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8831789}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8831789 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8831789}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Methionine biosynthesis]] | | [[Category: Methionine biosynthesis]] |
| | [[Category: Plp-dependent enzyme]] | | [[Category: Plp-dependent enzyme]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:50:59 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:53:45 2008'' |
Revision as of 17:53, 30 June 2008
Template:STRUCTURE 1cl1
CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI
Template:ABSTRACT PUBMED 8831789
About this Structure
1CL1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A., Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A, J Mol Biol. 1996 Sep 20;262(2):202-24. PMID:8831789
Page seeded by OCA on Mon Jun 30 20:53:45 2008
