1cl1
From Proteopedia
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| - | [[Image:1cl1.gif|left|200px]]<br /><applet load="1cl1" size=" | + | [[Image:1cl1.gif|left|200px]]<br /><applet load="1cl1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cl1, resolution 1.83Å" /> | caption="1cl1, resolution 1.83Å" /> | ||
'''CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI'''<br /> | '''CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CL1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with BCT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cystathionine_beta-lyase Cystathionine beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.8 4.4.1.8] Known structural/functional Sites: <scene name='pdbsite=PLA:Binding Site'>PLA</scene> and <scene name='pdbsite=PLB:Binding Site'>PLB</scene>. Full crystallographic information is available from [http:// | + | 1CL1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=BCT:'>BCT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cystathionine_beta-lyase Cystathionine beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.8 4.4.1.8] Known structural/functional Sites: <scene name='pdbsite=PLA:Binding+Site'>PLA</scene> and <scene name='pdbsite=PLB:Binding+Site'>PLB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CL1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: plp-dependent enzymes]] | [[Category: plp-dependent enzymes]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:34:44 2008'' |
Revision as of 07:34, 3 February 2008
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CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI
Overview
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.
About this Structure
1CL1 is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Cystathionine beta-lyase, with EC number 4.4.1.8 Known structural/functional Sites: and . 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
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