1iay

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[[Image:1iay.jpg|left|200px]]
[[Image:1iay.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1iay |SIZE=350|CAPTION= <scene name='initialview01'>1iay</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1iay", creates the "Structure Box" on the page.
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|SITE=
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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=AVG:2-AMINO-4-(2-AMINO-ETHOXY)-BUTYRIC+ACID'>AVG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</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/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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1iay| PDB=1iay | SCENE= }}
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|RELATEDENTRY=[[1iax|1IAX]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iay OCA], [http://www.ebi.ac.uk/pdbsum/1iay PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iay RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVG'''
'''CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVG'''
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[[Category: Li, N.]]
[[Category: Li, N.]]
[[Category: Xia, Y.]]
[[Category: Xia, Y.]]
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[[Category: protein-cofactor-inhibitor complex]]
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[[Category: Protein-cofactor-inhibitor complex]]
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[[Category: v6-dependent enzyme]]
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[[Category: V6-dependent enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:47:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:17:09 2008''
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Revision as of 16:47, 2 May 2008

Image:1iay.jpg

Template:STRUCTURE 1iay

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. 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 Page seeded by OCA on Fri May 2 19:47:21 2008

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