1iay
From Proteopedia
(New page: 200px<br /><applet load="1iay" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iay, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1iay.jpg|left|200px]]<br /><applet load="1iay" size=" | + | [[Image:1iay.jpg|left|200px]]<br /><applet load="1iay" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iay, resolution 2.7Å" /> | caption="1iay, resolution 2.7Å" /> | ||
'''CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVG'''<br /> | '''CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVG'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of tomato 1-aminocyclopropane-1-carboxylate synthase (ACS) | + | The structures of tomato 1-aminocyclopropane-1-carboxylate synthase (ACS) in complex with either cofactor pyridoxal-5'-phosphate (PLP) or both PLP and inhibitor aminoethoxyvinylglycine have been determined by x-ray crystallography. The structures showed good conservation of the catalytic residues, suggesting a similar catalytic mechanism for ACS and other PLP-dependent enzymes. However, the proximity of Tyr152 to the C-gamma-S bond of model substrate S-adenosylmethionine implies its critical role in the catalysis. The concerted accomplishment of catalysis by cofactor PLP and a protein residue, as proposed on the basis of the ACS structures in this paper, may represent a general scheme for the diversity of PLP-dependent catalyses. PLP-dependent enzymes have been categorized into four types of folds. A structural comparison revealed that a core fragment of ACS in fold type I is superimposable over tryptophan synthase beta subunit in fold type II and mouse ornithine decarboxylase in fold type III, thus suggesting a divergent evolution of PLP-dependent enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1IAY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum] with PLP and AVG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_synthase 1-aminocyclopropane-1-carboxylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.14 4.4.1.14] Full crystallographic information is available from [http:// | + | 1IAY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum] with <scene name='pdbligand=PLP:'>PLP</scene> and <scene name='pdbligand=AVG:'>AVG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_synthase 1-aminocyclopropane-1-carboxylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.14 4.4.1.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: v6-dependent enzyme]] | [[Category: v6-dependent enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:59 2008'' |
Revision as of 11:09, 21 February 2008
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CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVG
Overview
The structures of tomato 1-aminocyclopropane-1-carboxylate synthase (ACS) in complex with either cofactor pyridoxal-5'-phosphate (PLP) or both PLP and inhibitor aminoethoxyvinylglycine have been determined by x-ray crystallography. The structures showed good conservation of the catalytic residues, suggesting a similar catalytic mechanism for ACS and other PLP-dependent enzymes. However, the proximity of Tyr152 to the C-gamma-S bond of model substrate S-adenosylmethionine implies its critical role in the catalysis. The concerted accomplishment of catalysis by cofactor PLP and a protein residue, as proposed on the basis of the ACS structures in this paper, may represent a general scheme for the diversity of PLP-dependent catalyses. PLP-dependent enzymes have been categorized into four types of folds. A structural comparison revealed that a core fragment of ACS in fold type I is superimposable over tryptophan synthase beta subunit in fold type II and mouse ornithine decarboxylase in fold type III, thus suggesting a divergent evolution of PLP-dependent enzymes.
About this Structure
1IAY is a Single protein structure of sequence from Solanum lycopersicum with and as ligands. Active as 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14 Full crystallographic information is available from OCA.
Reference
Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms., Huai Q, Xia Y, Chen Y, Callahan B, Li N, Ke H, J Biol Chem. 2001 Oct 12;276(41):38210-6. Epub 2001 Jun 28. PMID:11431475
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