2bu3
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2bu3 |SIZE=350|CAPTION= <scene name='initialview01'>2bu3</scene>, resolution 1.40Å | |PDB= 2bu3 |SIZE=350|CAPTION= <scene name='initialview01'>2bu3</scene>, resolution 1.40Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Pignol, D.]] | [[Category: Pignol, D.]] | ||
[[Category: Vivares, D.]] | [[Category: Vivares, D.]] | ||
| - | [[Category: 3GC]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
[[Category: acyl-enzyme intermediate]] | [[Category: acyl-enzyme intermediate]] | ||
[[Category: alr0975]] | [[Category: alr0975]] | ||
| Line 38: | Line 38: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:11:50 2008'' |
Revision as of 23:11, 30 March 2008
| |||||||
| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Glutathione gamma-glutamylcysteinyltransferase, with EC number 2.3.2.15 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 02:11:50 2008
