1m7y

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[[Image:1m7y.png|left|200px]]
 
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==Crystal structure of apple ACC synthase in complex with L-aminoethoxyvinylglycine==
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The line below this paragraph, containing "STRUCTURE_1m7y", creates the "Structure Box" on the page.
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<StructureSection load='1m7y' size='340' side='right'caption='[[1m7y]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1m7y]] 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=1M7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M7Y FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.6&#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=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PPG:(2E,3E)-4-(2-AMINOETHOXY)-2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)IMINO]BUT-3-ENOIC+ACID'>PPG</scene></td></tr>
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{{STRUCTURE_1m7y| PDB=1m7y | SCENE= }}
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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=1m7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7y OCA], [https://pdbe.org/1m7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m7y RCSB], [https://www.ebi.ac.uk/pdbsum/1m7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7y 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/m7/1m7y_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=1m7y 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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The 1.6-A crystal structure of the covalent ketimine complex of apple 1-aminocyclopropane-1-carboxylate (ACC) synthase with the potent inhibitor l-aminoethoxyvinylglycine (AVG) is described. ACC synthase catalyzes the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. AVG is widely used in plant physiology studies to inhibit the activity of ACC synthase. The structural assignment is supported by the fact that the complex absorbs maximally at 341 nm. These results are not in accord with the recently reported crystal structure of the tomato ACC synthase AVG complex, which claims that the inhibitor only associates noncovalently. The rate constant for the association of AVG with apple ACC synthase was determined by stopped-flow spectrophotometry (2.1 x 10(5) m(-1) s(-1)) and by the rate of loss of enzyme activity (1.1 x 10(5) m(-1) s(-1)). The dissociation rate constant determined by activity recovery is 2.4 x 10(-6) s(-1). Thus, the calculated K(d) value is 10-20 pm.
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===Crystal structure of apple ACC synthase in complex with L-aminoethoxyvinylglycine===
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Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate.,Capitani G, McCarthy DL, Gut H, Grutter MG, Kirsch JF J Biol Chem. 2002 Dec 20;277(51):49735-42. Epub 2002 Sep 11. PMID:12228256<ref>PMID:12228256</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12228256}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1m7y" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12228256 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12228256}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[1m7y]] is a 1 chain structure with 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=1M7Y OCA].
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[[Category: Malus domestica]]
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[[Category: Capitani G]]
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==Reference==
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[[Category: Gruetter MG]]
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<ref group="xtra">PMID:012228256</ref><references group="xtra"/>
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[[Category: Gut H]]
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[[Category: 1-aminocyclopropane-1-carboxylate synthase]]
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[[Category: Kirsch JF]]
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[[Category: Malus x domestica]]
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[[Category: McCarthy D]]
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[[Category: Capitani, G.]]
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[[Category: Gruetter, M G.]]
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[[Category: Gut, H.]]
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[[Category: Kirsch, J F.]]
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[[Category: McCarthy, D.]]
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[[Category: Ethylene biosynthesis]]
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[[Category: Fruit ripening]]
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[[Category: Lyase]]
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[[Category: Pyridoxal phosphate]]
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Current revision

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

PDB ID 1m7y

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