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1ajs

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[[Image:1ajs.jpg|left|200px]]
 
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{{Structure
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==REFINEMENT AND COMPARISON OF THE CRYSTAL STRUCTURES OF PIG CYTOSOLIC ASPARTATE AMINOTRANSFERASE AND ITS COMPLEX WITH 2-METHYLASPARTATE==
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|PDB= 1ajs |SIZE=350|CAPTION= <scene name='initialview01'>1ajs</scene>, resolution 1.60&Aring;
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<StructureSection load='1ajs' size='340' side='right'caption='[[1ajs]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE= <scene name='pdbsite=ACT:Coenzyme+Binding+Sites'>ACT</scene> and <scene name='pdbsite=AXT:Substrate+Binding+Sites'>AXT</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>, <scene name='pdbligand=PLA:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-2-METHYL-SUCCINIC+ACID'>PLA</scene>
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<table><tr><td colspan='2'>[[1ajs]] 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=1AJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AJS FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span>
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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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|GENE=
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<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>, <scene name='pdbligand=PLA:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-2-METHYL-SUCCINIC+ACID'>PLA</scene></td></tr>
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|DOMAIN=
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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=1ajs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ajs OCA], [https://pdbe.org/1ajs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ajs RCSB], [https://www.ebi.ac.uk/pdbsum/1ajs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ajs ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ajs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ajs OCA], [http://www.ebi.ac.uk/pdbsum/1ajs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ajs RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AATC_PIG AATC_PIG] Plays a key role in amino acid metabolism.
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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/aj/1ajs_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=1ajs ConSurf].
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<div style="clear:both"></div>
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'''REFINEMENT AND COMPARISON OF THE CRYSTAL STRUCTURES OF PIG CYTOSOLIC ASPARTATE AMINOTRANSFERASE AND ITS COMPLEX WITH 2-METHYLASPARTATE'''
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==See Also==
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*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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1AJS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJS OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9211866 9211866]
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[[Category: Aspartate transaminase]]
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[[Category: Protein complex]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Arnone, A.]]
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[[Category: Arnone A]]
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[[Category: Hyde, C C.]]
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[[Category: Hyde CC]]
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[[Category: Metzler, C M.]]
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[[Category: Metzler CM]]
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[[Category: Metzler, D E.]]
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[[Category: Metzler DE]]
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[[Category: Rhee, S.]]
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[[Category: Rhee S]]
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[[Category: Rogers, P H.]]
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[[Category: Rogers PH]]
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[[Category: Silva, M M.]]
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[[Category: Silva MM]]
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[[Category: aminotransferase]]
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[[Category: cytosolic aspartate aminotransferase]]
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[[Category: in the presence of ligand 2-methylaspartate]]
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[[Category: pig]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:41:48 2008''
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Current revision

REFINEMENT AND COMPARISON OF THE CRYSTAL STRUCTURES OF PIG CYTOSOLIC ASPARTATE AMINOTRANSFERASE AND ITS COMPLEX WITH 2-METHYLASPARTATE

PDB ID 1ajs

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