1ynu

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[[Image:1ynu.gif|left|200px]]<br /><applet load="1ynu" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ynu.gif|left|200px]]
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caption="1ynu, resolution 2.25&Aring;" />
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'''Crystal structure of apple ACC synthase in complex with L-vinylglycine'''<br />
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{{Structure
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|PDB= 1ynu |SIZE=350|CAPTION= <scene name='initialview01'>1ynu</scene>, resolution 2.25&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PY4:2-[O-PHOSPHONOPYRIDOXYL]-AMINO-+BUTYRIC+ACID'>PY4</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|ACTIVITY= [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]
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|GENE= ACS-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3750 Malus x domestica])
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}}
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'''Crystal structure of apple ACC synthase in complex with L-vinylglycine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YNU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Malus_x_domestica Malus x domestica] with <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=PY4:'>PY4</scene> and <scene name='pdbligand=TRS:'>TRS</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=1YNU OCA].
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1YNU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Malus_x_domestica Malus x domestica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNU OCA].
==Reference==
==Reference==
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Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine., Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grutter MG, FEBS Lett. 2005 Apr 25;579(11):2458-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15848188 15848188]
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Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine., Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grutter MG, FEBS Lett. 2005 Apr 25;579(11):2458-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15848188 15848188]
[[Category: 1-aminocyclopropane-1-carboxylate synthase]]
[[Category: 1-aminocyclopropane-1-carboxylate synthase]]
[[Category: Malus x domestica]]
[[Category: Malus x domestica]]
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[[Category: lyase]]
[[Category: lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:25:15 2008''

Revision as of 13:25, 20 March 2008


PDB ID 1ynu

Drag the structure with the mouse to rotate
, resolution 2.25Å
Ligands: , , and
Gene: ACS-1 (Malus x domestica)
Activity: 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14
Coordinates: save as pdb, mmCIF, xml



Crystal structure of apple ACC synthase in complex with L-vinylglycine


Overview

L-Vinylglycine (L-VG) is both a substrate for and a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate (ACC) synthase. The ratio of the rate constants for catalytic conversion to alpha-ketobutyrate and ammonia to inactivation is 500/1. The crystal structure of the covalent adduct of the inactivated enzyme was determined at 2.25 Angstroms resolution. The active site contains an external aldimine of the adduct of L-VG with the pyridoxal 5'-phosphate cofactor. The side chain gamma-carbon of L-VG is covalently bound to the epsilon-amino group of Lys273. This species corresponds to one of the two alternatives proposed by Feng and Kirsch [Feng, L. and Kirsch, J.F. (2000) L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthase. Biochemistry 39, 2436-2444] and presumably results from Michael addition to a vinylglycine ketimine intermediate.

About this Structure

1YNU is a Single protein structure of sequence from Malus x domestica. Full crystallographic information is available from OCA.

Reference

Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine., Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grutter MG, FEBS Lett. 2005 Apr 25;579(11):2458-62. PMID:15848188

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