2btw
From Proteopedia
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| - | [[Image:2btw.gif|left|200px]]<br /> | + | [[Image:2btw.gif|left|200px]]<br /><applet load="2btw" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2btw" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2btw, resolution 2.00Å" /> | caption="2btw, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF ALR0975'''<br /> | '''CRYSTAL STRUCTURE OF ALR0975'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BTW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. 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] | + | 2BTW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BTW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:58:20 2007'' |
Revision as of 16:48, 18 December 2007
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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. with CA as ligand. 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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