1j0c: Difference between revisions

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-{{STRUCTURE_1j0c|  PDB=1j0c  |  SCENE=  }}
+==ACC deaminase mutated to catalytic residue==
-===ACC deaminase mutated to catalytic residue===
+<StructureSection load='1j0c' size='340' side='right' caption='[[1j0c]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
-{{ABSTRACT_PUBMED_12882962}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1j0c]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J0C FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f2d|1f2d]], [[1j0a|1j0a]], [[1j0b|1j0b]], [[1j0d|1j0d]], [[1j0e|1j0e]]</td></tr>
+<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_deaminase 1-aminocyclopropane-1-carboxylate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.7 3.5.99.7] </span></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j0c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j0c RCSB], [http://www.ebi.ac.uk/pdbsum/1j0c PDBsum]</span></td></tr>
+<table>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j0/1j0c_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The pyridoxal 5'-phosphate-dependent enzymes have been evolved to catalyze diverse substrates and to cause the reaction to vary. 1-Aminocyclopropane-1-carboxylate deaminase catalyzes the cyclopropane ring-opening reaction followed by deamination specifically. Since it was discovered in 1978, the enzyme has been widely investigated from the mechanistic and physiological viewpoints because the substrate is a precursor of the plant hormone ethylene and the enzymatic reaction includes a cyclopropane ring-opening. We have previously reported the crystal structure of the native enzyme. Here we report the crystal structures of the two reaction intermediates created by the mutagenesis complexed with the substrate. The substrate was validated in the active site of two forms: 1). covalent-bonded external aldimine with the coenzyme in the K51T form and 2). the non-covalent interaction around the coenzyme in the Y295F form. The orientations of the substrate in both structures were quite different form each other. In concert with other site-specific mutation experiments, this experiment revealed the ingenious and unique strategies that are used to achieve the specific activity. The substrate incorporated into the active site is reactivated by a two-phenol charge relay system to lead to the formation of a Schiff base with the coenzyme. The catalytic Lys51 residue may play a novel role to abstract the methylene proton from the substrate in cooperation with other factors, the carboxylate group of the substrate and the electron-adjusting apparatuses of the coenzyme.
-==Function==
+Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction.,Ose T, Fujino A, Yao M, Watanabe N, Honma M, Tanaka I J Biol Chem. 2003 Oct 17;278(42):41069-76. Epub 2003 Jul 26. PMID:12882962<ref>PMID:12882962</ref>
-[[http://www.uniprot.org/uniprot/1A1D_WILSA 1A1D_WILSA]] Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[1j0c]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J0C OCA].
+</div>
-==Reference==
+==See Also==
-<ref group="xtra">PMID:012882962</ref><references group="xtra"/><references/>
+*[[Deaminase|Deaminase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: 1-aminocyclopropane-1-carboxylate deaminase]]
 [[Category: Fujino, A.]]