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1ynu

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(New page: 200px<br /><applet load="1ynu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ynu, resolution 2.25&Aring;" /> '''Crystal structure of...)
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[[Image:1ynu.gif|left|200px]]<br /><applet load="1ynu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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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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==Overview==
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==Crystal structure of apple ACC synthase in complex with L-vinylglycine==
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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.
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<StructureSection load='1ynu' size='340' side='right'caption='[[1ynu]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ynu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Malus_domestica Malus domestica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YNU FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PY4:2-[O-PHOSPHONOPYRIDOXYL]-AMINO-+BUTYRIC+ACID'>PY4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ynu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ynu OCA], [https://pdbe.org/1ynu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ynu RCSB], [https://www.ebi.ac.uk/pdbsum/1ynu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ynu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/1A1C_MALDO 1A1C_MALDO] Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yn/1ynu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ynu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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:15848188<ref>PMID:15848188</ref>
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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 NI, K, PY4 and TRS 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YNU OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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[[Category: 1-aminocyclopropane-1-carboxylate synthase]]
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<div class="pdbe-citations 1ynu" style="background-color:#fffaf0;"></div>
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[[Category: Malus x domestica]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Capitani, G.]]
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__TOC__
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[[Category: Eliot, A.C.]]
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</StructureSection>
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[[Category: Grutter, M.G.]]
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[[Category: Large Structures]]
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[[Category: Kirsch, J.F.]]
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[[Category: Malus domestica]]
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[[Category: Tschopp, M.]]
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[[Category: Capitani G]]
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[[Category: K]]
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[[Category: Eliot AC]]
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[[Category: NI]]
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[[Category: Grutter MG]]
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[[Category: PY4]]
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[[Category: Kirsch JF]]
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[[Category: TRS]]
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[[Category: Tschopp M]]
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[[Category: lyase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:56:17 2007''
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Current revision

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

PDB ID 1ynu

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