This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2btw
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2btw.gif|left|200px]] | [[Image:2btw.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2btw", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_2btw| PDB=2btw | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''CRYSTAL STRUCTURE OF ALR0975''' | '''CRYSTAL STRUCTURE OF ALR0975''' | ||
| Line 29: | Line 26: | ||
[[Category: Pignol, D.]] | [[Category: Pignol, D.]] | ||
[[Category: Vivares, D.]] | [[Category: Vivares, D.]] | ||
| - | [[Category: | + | [[Category: Alr0975]] |
| - | [[Category: | + | [[Category: Cysteine protease]] |
| - | [[Category: | + | [[Category: Glutathione metabolism]] |
| - | [[Category: | + | [[Category: Nostoc]] |
| - | [[Category: | + | [[Category: Pc]] |
| - | [[Category: | + | [[Category: Phytochelatin synthase]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:47:31 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:47, 3 May 2008
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.. 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 Sat May 3 20:47:31 2008
