2bu3
From Proteopedia
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| - | [[Image:2bu3.gif|left|200px]]<br /><applet load="2bu3" size=" | + | [[Image:2bu3.gif|left|200px]]<br /><applet load="2bu3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bu3, resolution 1.40Å" /> | caption="2bu3, resolution 1.40Å" /> | ||
'''ACYL-ENZYME INTERMEDIATE BETWEEN ALR0975 AND GLUTATHIONE AT PH 3.4'''<br /> | '''ACYL-ENZYME INTERMEDIATE BETWEEN ALR0975 AND GLUTATHIONE AT PH 3.4'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with CL, CA and 3GC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Ca Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2BU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=3GC:'>3GC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BU3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:27:46 2008'' |
Revision as of 08:27, 3 February 2008
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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. with , and as ligands. Active as Glutathione gamma-glutamylcysteinyltransferase, with EC number 2.3.2.15 Known structural/functional Site: . 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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