1m4n

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(New page: 200px<br /><applet load="1m4n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m4n, resolution 2.01&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1m4n.jpg|left|200px]]<br /><applet load="1m4n" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m4n, resolution 2.01&Aring;" />
 
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'''CRYSTAL STRUCTURE OF APPLE ACC SYNTHASE IN COMPLEX WITH [2-(AMINO-OXY)ETHYL](5'-DEOXYADENOSIN-5'-YL)(METHYL)SULFONIUM'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF APPLE ACC SYNTHASE IN COMPLEX WITH [2-(AMINO-OXY)ETHYL](5'-DEOXYADENOSIN-5'-YL)(METHYL)SULFONIUM==
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The crystal structure of 1-aminocyclopropane-1-carboxylate (ACC) synthase, in complex with the substrate analogue, [2-(amino-oxy)ethyl](5'-deoxyadenosin-5'-yl)(methyl)sulfonium (AMA) was, determined at 2.01-A resolution. The crystallographic results show that a, covalent adduct (oxime) is formed between AMA (an amino-oxy analogue of, the natural substrate S-adenosyl-L-methionine (SAM)) and the pyridoxal, 5'-phosphate (PLP) cofactor of ACC synthase. The oxime formation is, supported by spectroscopic data. The ACC synthase-AMA structure provides, reliable and detailed information on the binding mode of the natural, substrate of ACC synthase and complements previous structural and, functional work on this enzyme.
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<StructureSection load='1m4n' size='340' side='right'caption='[[1m4n]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1m4n]] 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=1M4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M4N 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]] 2.01&#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=AAD:(2-AMINOOXY-ETHYL)-[5-(6-AMINO-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDRO-FURAN-2-YLMETHYL]-METHYL-SULFONIUM'>AAD</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <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=1m4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4n OCA], [https://pdbe.org/1m4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m4n RCSB], [https://www.ebi.ac.uk/pdbsum/1m4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m4n 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/m4/1m4n_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=1m4n 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 crystal structure of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with the substrate analogue [2-(amino-oxy)ethyl](5'-deoxyadenosin-5'-yl)(methyl)sulfonium (AMA) was determined at 2.01-A resolution. The crystallographic results show that a covalent adduct (oxime) is formed between AMA (an amino-oxy analogue of the natural substrate S-adenosyl-L-methionine (SAM)) and the pyridoxal 5'-phosphate (PLP) cofactor of ACC synthase. The oxime formation is supported by spectroscopic data. The ACC synthase-AMA structure provides reliable and detailed information on the binding mode of the natural substrate of ACC synthase and complements previous structural and functional work on this enzyme.
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==About this Structure==
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Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding.,Capitani G, Eliot AC, Gut H, Khomutov RM, Kirsch JF, Grutter MG Biochim Biophys Acta. 2003 Apr 11;1647(1-2):55-60. PMID:12686108<ref>PMID:12686108</ref>
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1M4N 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, AAD and MES 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=1M4N 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 in complex with an amino-oxy analogue of the substrate: implications for substrate binding., Capitani G, Eliot AC, Gut H, Khomutov RM, Kirsch JF, Grutter MG, Biochim Biophys Acta. 2003 Apr 11;1647(1-2):55-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12686108 12686108]
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</div>
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[[Category: 1-aminocyclopropane-1-carboxylate synthase]]
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<div class="pdbe-citations 1m4n" 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: Gut, H.]]
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[[Category: Malus domestica]]
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[[Category: Khomutov, R.M.]]
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[[Category: Capitani G]]
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[[Category: Kirsch, J.F.]]
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[[Category: Eliot AC]]
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[[Category: AAD]]
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[[Category: Grutter MG]]
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[[Category: MES]]
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[[Category: Gut H]]
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[[Category: PLP]]
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[[Category: Khomutov RM]]
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[[Category: ethylene biosynthesis]]
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[[Category: Kirsch JF]]
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[[Category: fruit ripening]]
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[[Category: pyridoxal phosphate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:08:42 2007''
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Current revision

CRYSTAL STRUCTURE OF APPLE ACC SYNTHASE IN COMPLEX WITH [2-(AMINO-OXY)ETHYL](5'-DEOXYADENOSIN-5'-YL)(METHYL)SULFONIUM

PDB ID 1m4n

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