2btw
From Proteopedia
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==Overview== | ==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 .. | + | 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 gamma-glutamyl cysteine acyl-enzyme, intermediate stabilized in a cavity of the protein adjacent to a second, putative GSH binding site. GSH hydrolase and PCS activities of the enzyme, are discussed in the light of both structures. |
==About this Structure== | ==About this Structure== | ||
| - | 2BTW is a | + | 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== | ||
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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 Mon Nov 5 15:27:00 2007'' |
Revision as of 13:21, 5 November 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 gamma-glutamyl cysteine acyl-enzyme, intermediate stabilized in a cavity of the protein adjacent to a second, putative GSH binding site. GSH hydrolase and PCS activities of the enzyme, are discussed in the light of both structures.
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
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