1ajr: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[1ajr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AJR FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ajr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ajr OCA], [https://pdbe.org/1ajr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ajr RCSB], [https://www.ebi.ac.uk/pdbsum/1ajr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ajr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/AATC_PIG AATC_PIG]] Plays a key role in amino acid metabolism.
+[https://www.uniprot.org/uniprot/AATC_PIG AATC_PIG] Plays a key role in amino acid metabolism.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1ajr ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Two high resolution crystal structures of cytosolic aspartate aminotransferase from pig heart provide additional insights into the stereochemical mechanism for ligand-induced conformational changes in this enzyme. Structures of the homodimeric native structure and its complex with the substrate analog 2-methylaspartate have been refined, respectively, with 1.74-A x-ray diffraction data to an R value of 0.170, and with 1.6-A data to an R value of 0.173. In the presence of 2-methylaspartate, one of the subunits (subunit 1) shows a ligand-induced conformational change that involves a large movement of the small domain (residues 12-49 and 327-412) to produce a "closed" conformation. No such transition is observed in the other subunit (subunit 2), because crystal lattice contacts lock it in an "open" conformation like that adopted by subunit 1 in the absence of substrate. By comparing the open and closed forms of cAspAT, we propose a stereochemical mechanism for the open-to-closed transition that involves the electrostatic neutralization of two active site arginine residues by the negative charges of the incoming substrate, a large change in the backbone (phi,psi) conformational angles of two key glycine residues, and the entropy-driven burial of a stretch of hydrophobic residues on the N-terminal helix. The calculated free energy for the burial of this "hydrophobic plug" appears to be sufficient to serve as the driving force for domain closure.
-Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate.,Rhee S, Silva MM, Hyde CC, Rogers PH, Metzler CM, Metzler DE, Arnone A J Biol Chem. 1997 Jul 11;272(28):17293-302. PMID:9211866<ref>PMID:9211866</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1ajr" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Aspartate transaminase]]
 [[Category: Large Structures]]
 [[Category: Sus scrofa]]
-[[Category: Arnone, A]]
+[[Category: Arnone A]]
-[[Category: Hyde, C C]]
+[[Category: Hyde CC]]
-[[Category: Metzler, C M]]
+[[Category: Metzler CM]]
-[[Category: Metzler, D E]]
+[[Category: Metzler DE]]
-[[Category: Rhee, S]]
+[[Category: Rhee S]]
-[[Category: Rogers, P H]]
+[[Category: Rogers PH]]
-[[Category: Silva, M M]]
+[[Category: Silva MM]]
-[[Category: Aminotransferase]]
-[[Category: Cytosolic aspartate aminotransferase]]
-[[Category: Homodimer in the absence of ligand]]
-[[Category: Pig]]