1oxp

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[[Image:1oxp.jpg|left|200px]]
 
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{{Structure
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==ASPARTATE AMINOTRANSFERASE, H-ASP COMPLEX, CLOSED CONFORMATION==
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|PDB= 1oxp |SIZE=350|CAPTION= <scene name='initialview01'>1oxp</scene>, resolution 2.5&Aring;
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<StructureSection load='1oxp' size='340' side='right'caption='[[1oxp]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=IK2:4&#39;-DEOXY-4&#39;-ACETYLYAMINO-PYRIDOXAL-5&#39;-PHOSPHATE'>IK2</scene>
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<table><tr><td colspan='2'>[[1oxp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OXP 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]] 2.5&#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=IK2:4-DEOXY-4-ACETYLYAMINO-PYRIDOXAL-5-PHOSPHATE'>IK2</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=1oxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxp OCA], [https://pdbe.org/1oxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxp RCSB], [https://www.ebi.ac.uk/pdbsum/1oxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxp 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=1oxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxp OCA], [http://www.ebi.ac.uk/pdbsum/1oxp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oxp RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AATM_CHICK AATM_CHICK] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. May facilitate cellular uptake of long-chain free fatty acids (By similarity).
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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/ox/1oxp_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=1oxp ConSurf].
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<div style="clear:both"></div>
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'''ASPARTATE AMINOTRANSFERASE, H-ASP COMPLEX, CLOSED CONFORMATION'''
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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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The interaction of mitochondrial aspartate aminotransferase with hydroxylamine and five derivatives (in which the hydroxyl hydrogen is replaced by the side chain of naturally occurring amino acids) was investigated by X-ray diffraction as well as by kinetic and spectral measurements with the enzyme in solution. The inhibitors react with pyridoxal 5'-phosphate in the enzyme active site, both in solution and in the crystalline state, in a reversible single-step reaction forming spectrally distinct oxime adducts. Dissociation constants determined in solution range from 10(-8) M to 10(-6) M depending on the nature of the side-chain group. The crystal structures of the adducts of mitochondrial aspartate aminotransferase with the monocarboxylic analogue of L-aspartate in the open and closed enzyme conformation were determined at 0.23-nm and 0.25-nm resolution, respectively. This inhibitor binds to both the open and closed crystal forms of the enzyme without disturbing the crystalline order. Small differences in the conformation of the cofactor pyridoxal phosphate were detected between the omega-carboxylate of the inhibitor and Arg292 of the neighbouring subunit is mainly responsible for the attainment of near-coplanarity of the aldimine bond with the pyridine ring in the oxime adducts. Studies with a fluorescent probe aimed to detect shifts in the open/closed conformational equilibrium of the enzyme in oxime complexes showed that the hydroxylamine-derived inhibitors, even those containing a carboxylate group, do not induce the 'domain closure' in solution. This is probably due to the absence of the alpha-carboxylate group in the monocarboxylic hydroxylamine-derived inhibitors, emphasizing that both carboxylates of the substrates L-Asp and L-Glu are essential for stabilizing the closed form of aspartate aminotransferase.
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==About this Structure==
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1OXP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXP OCA].
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==Reference==
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Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase., Markovic-Housley Z, Schirmer T, Hohenester E, Khomutov AR, Khomutov RM, Karpeisky MY, Sandmeier E, Christen P, Jansonius JN, Eur J Biochem. 1996 Mar 15;236(3):1025-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8665890 8665890]
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[[Category: Aspartate transaminase]]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hohenester, E.]]
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[[Category: Hohenester E]]
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[[Category: Jansonius, J N.]]
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[[Category: Jansonius JN]]
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[[Category: Schirmer, T.]]
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[[Category: Schirmer T]]
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[[Category: aminotransferase]]
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[[Category: hydroxylamine derived inhibitor]]
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[[Category: vitamin b6]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:51:51 2008''
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Current revision

ASPARTATE AMINOTRANSFERASE, H-ASP COMPLEX, CLOSED CONFORMATION

PDB ID 1oxp

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