2bu3

From Proteopedia

Revision as of 14:43, 30 October 2007

ACYL-ENZYME INTERMEDIATE BETWEEN ALR0975 AND GLUTATHIONE AT PH 3.4

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

2BU3 is a [Single protein] structure of sequence from [Anabaena sp.] with CL, CA and 3GC as [ligands]. 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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