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2btw
From Proteopedia
(New page: 200px<br /> <applet load="2btw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2btw, resolution 2.00Å" /> '''CRYSTAL STRUCTURE O...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2BTW is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]] with CA 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=2.3.2.15 2.3.2.15]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BTW OCA]]. | + | 2BTW is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Glutathione_gamma-glutamylcysteinyltransferase Glutathione gamma-glutamylcysteinyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.15 2.3.2.15]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BTW OCA]]. |
==Reference== | ==Reference== | ||
A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis., Vivares D, Arnoux P, Pignol D, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18848-53. Epub 2005 Dec 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16339904 16339904] | A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis., Vivares D, Arnoux P, Pignol D, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18848-53. Epub 2005 Dec 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16339904 16339904] | ||
[[Category: Anabaena sp.]] | [[Category: Anabaena sp.]] | ||
| + | [[Category: Glutathione gamma-glutamylcysteinyltransferase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Arnoux, P.]] | [[Category: Arnoux, P.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 14:23:42 2007'' |
Revision as of 12:18, 30 October 2007
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CRYSTAL STRUCTURE OF ALR0975
Overview
Phytochelatin synthase (PCS) is a key enzyme for heavy-metal, detoxification in plants. PCS catalyzes the production of glutathione, (GSH)-derived peptides (called phytochelatins or PCs) that bind, heavy-metal ions before vacuolar sequestration. The enzyme can also, hydrolyze GSH and GS-conjugated xenobiotics. In the cyanobacterium Nostoc, the enzyme (NsPCS) contains only the catalytic domain of the eukaryotic, synthase and can act as a GSH hydrolase and weakly as a peptide ligase., The crystal structure of NsPCS in its native form solved at a 2.0-A, resolution shows that NsPCS is a dimer that belongs to the papain, superfamily of cysteine proteases, with a conserved catalytic machinery., Moreover, the structure of the protein solved as a complex with GSH at a, 1.4-A resolution reveals a ... [(full description)]
About this Structure
2BTW is a [Protein complex] structure of sequences from [Anabaena sp.] with CA as [ligand]. Active as [Glutathione gamma-glutamylcysteinyltransferase], with EC number [2.3.2.15]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis., Vivares D, Arnoux P, Pignol D, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18848-53. Epub 2005 Dec 9. PMID:16339904
Page seeded by OCA on Tue Oct 30 14:23:42 2007
