1iay: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iay]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IAY FirstGlance]. <br> | <table><tr><td colspan='2'>[[1iay]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IAY FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AVG:2-AMINO-4-(2-AMINO-ETHOXY)-BUTYRIC+ACID'>AVG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AVG:2-AMINO-4-(2-AMINO-ETHOXY)-BUTYRIC+ACID'>AVG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iax|1iax]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iax|1iax]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1iay RCSB], [http://www.ebi.ac.uk/pdbsum/1iay PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1iay RCSB], [http://www.ebi.ac.uk/pdbsum/1iay PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: 1-aminocyclopropane-1-carboxylate synthase]] | [[Category: 1-aminocyclopropane-1-carboxylate synthase]] | ||
[[Category: Solanum lycopersicum]] | [[Category: Solanum lycopersicum]] | ||
[[Category: Callahan, B | [[Category: Callahan, B]] | ||
[[Category: Chen, Y | [[Category: Chen, Y]] | ||
[[Category: Huai, Q | [[Category: Huai, Q]] | ||
[[Category: Ke, H | [[Category: Ke, H]] | ||
[[Category: Li, N | [[Category: Li, N]] | ||
[[Category: Xia, Y | [[Category: Xia, Y]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Protein-cofactor-inhibitor complex]] | [[Category: Protein-cofactor-inhibitor complex]] | ||
[[Category: V6-dependent enzyme]] | [[Category: V6-dependent enzyme]] | ||
Revision as of 12:29, 2 January 2015
CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVGCRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVG
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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