2btw: Difference between revisions

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[[Image:2btw.gif|left|200px]]
{{Seed}}
[[Image:2btw.png|left|200px]]


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{{STRUCTURE_2btw|  PDB=2btw  |  SCENE=  }}  
{{STRUCTURE_2btw|  PDB=2btw  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF ALR0975'''
===CRYSTAL STRUCTURE OF ALR0975===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_16339904}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_16339904}}


==About this Structure==
==About this Structure==
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[[Category: Phytochelatin synthase]]
[[Category: Phytochelatin synthase]]
[[Category: Transferase]]
[[Category: Transferase]]
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Revision as of 09:03, 28 July 2008

File:2btw.png

Template:STRUCTURE 2btw

CRYSTAL STRUCTURE OF ALR0975

Template:ABSTRACT PUBMED 16339904

About this Structure

2BTW is a Protein complex structure of sequences from Anabaena sp.. 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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