2bu3

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[[Image:2bu3.gif|left|200px]]
[[Image:2bu3.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2bu3 |SIZE=350|CAPTION= <scene name='initialview01'>2bu3</scene>, resolution 1.40&Aring;
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The line below this paragraph, containing "STRUCTURE_2bu3", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=3GC:GAMMA-GLUTAMYLCYSTEINE'>3GC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2bu3| PDB=2bu3 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bu3 OCA], [http://www.ebi.ac.uk/pdbsum/2bu3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bu3 RCSB]</span>
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}}
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'''ACYL-ENZYME INTERMEDIATE BETWEEN ALR0975 AND GLUTATHIONE AT PH 3.4'''
'''ACYL-ENZYME INTERMEDIATE BETWEEN ALR0975 AND GLUTATHIONE AT PH 3.4'''
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[[Category: Pignol, D.]]
[[Category: Pignol, D.]]
[[Category: Vivares, D.]]
[[Category: Vivares, D.]]
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[[Category: acyl-enzyme intermediate]]
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[[Category: Acyl-enzyme intermediate]]
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[[Category: alr0975]]
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[[Category: Alr0975]]
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[[Category: cysteine protease]]
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[[Category: Cysteine protease]]
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[[Category: glutathione metabolism]]
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[[Category: Glutathione metabolism]]
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[[Category: nostoc]]
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[[Category: Nostoc]]
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[[Category: pc]]
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[[Category: Pc]]
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[[Category: phytochelatin synthase]]
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[[Category: Phytochelatin synthase]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:47:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:11:50 2008''
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Revision as of 17:47, 3 May 2008

Template:STRUCTURE 2bu3

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 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

2BU3 is a Single protein structure of sequence 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 20:47:55 2008

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