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1b8g

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(New page: 200px<br /><applet load="1b8g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b8g, resolution 2.37&Aring;" /> '''1-AMINOCYCLOPROPANE-...)
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[[Image:1b8g.gif|left|200px]]<br /><applet load="1b8g" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1b8g, resolution 2.37&Aring;" />
 
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'''1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE'''<br />
 
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==Overview==
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==1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE==
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The 2.4 A crystal structure of the vitamin B6-dependent enzyme, 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme, catalyses 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. ACC synthase has 15 %, sequence identity with the well-studied aspartate aminotransferase, and a, completely different catalytic activity yet the overall folds and the, active sites are very similar. The new structure together with available, biochemical data enables a comparative mechanistic analysis that largely, explains the catalytic roles of the conserved and non-conserved active, site residues. An external aldimine reaction intermediate (external, aldimine with ACC, i.e. with the product) has been modeled. The new, structure provides a basis for the rational design of inhibitors with, broad agricultural applications.
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<StructureSection load='1b8g' size='340' side='right'caption='[[1b8g]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1b8g]] is a 2 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=1B8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B8G 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]] 2.37&#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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=1b8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8g OCA], [https://pdbe.org/1b8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b8g RCSB], [https://www.ebi.ac.uk/pdbsum/1b8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b8g 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/b8/1b8g_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=1b8g 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 2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses 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. ACC synthase has 15 % sequence identity with the well-studied aspartate aminotransferase, and a completely different catalytic activity yet the overall folds and the active sites are very similar. The new structure together with available biochemical data enables a comparative mechanistic analysis that largely explains the catalytic roles of the conserved and non-conserved active site residues. An external aldimine reaction intermediate (external aldimine with ACC, i.e. with the product) has been modeled. The new structure provides a basis for the rational design of inhibitors with broad agricultural applications.
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==About this Structure==
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Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene.,Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN J Mol Biol. 1999 Dec 3;294(3):745-56. PMID:10610793<ref>PMID:10610793</ref>
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1B8G 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 PLP as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1B8G 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 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene., Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN, J Mol Biol. 1999 Dec 3;294(3):745-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10610793 10610793]
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</div>
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[[Category: 1-aminocyclopropane-1-carboxylate synthase]]
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<div class="pdbe-citations 1b8g" 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: Feng, L.]]
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</StructureSection>
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[[Category: Hohenester, E.]]
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[[Category: Large Structures]]
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[[Category: Jansonius, J.N.]]
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[[Category: Malus domestica]]
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[[Category: Kirsch, J.F.]]
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[[Category: Capitani G]]
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[[Category: Storici, P.]]
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[[Category: Feng L]]
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[[Category: PLP]]
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[[Category: Hohenester E]]
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[[Category: ethylene biosynthesis]]
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[[Category: Jansonius JN]]
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[[Category: Kirsch JF]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:26:59 2007''
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[[Category: Storici P]]

Current revision

1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE

PDB ID 1b8g

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