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1cl1
From Proteopedia
(New page: 200px<br /> <applet load="1cl1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cl1, resolution 1.83Å" /> '''CYSTATHIONINE BETA-...) |
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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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.8 4.4.1.8]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CL1 OCA]]. | + | 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]]. Structure known Active Sites: PLA and PLB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CL1 OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8831789 8831789] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8831789 8831789] | ||
| + | [[Category: Cystathionine beta-lyase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: plp-dependent enzymes]] | [[Category: plp-dependent enzymes]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:17:48 2007'' |
Revision as of 10:13, 30 October 2007
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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 ... [(full description)]
About this Structure
1CL1 is a [Single protein] structure of sequence from [Escherichia coli] with BCT as [ligand]. Active as [Cystathionine beta-lyase], with EC number [4.4.1.8]. Structure known Active Sites: PLA and PLB. 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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