1tat: Difference between revisions

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[[Image:1tat.png|left|200px]]


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==CRYSTALLINE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE EXISTS IN ONLY TWO CONFORMATIONS==
The line below this paragraph, containing "STRUCTURE_1tat", creates the "Structure Box" on the page.
<StructureSection load='1tat' size='340' side='right'caption='[[1tat]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1tat]] is a 2 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=1TAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TAT FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
{{STRUCTURE_1tat| PDB=1tat |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tat OCA], [https://pdbe.org/1tat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tat RCSB], [https://www.ebi.ac.uk/pdbsum/1tat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tat ProSAT]</span></td></tr>
</table>
== Function ==
[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).
== 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/ta/1tat_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/main_output.php?pdb_ID=1tat ConSurf].
<div style="clear:both"></div>


===CRYSTALLINE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE EXISTS IN ONLY TWO CONFORMATIONS===
==See Also==
 
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
 
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{{ABSTRACT_PUBMED_8120903}}
 
==About this Structure==
1TAT 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=1TAT OCA].
 
==Reference==
Crystalline mitochondrial aspartate aminotransferase exists in only two conformations., Hohenester E, Jansonius JN, J Mol Biol. 1994 Mar 4;236(4):963-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8120903 8120903]
[[Category: Aspartate transaminase]]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hohenester, E.]]
[[Category: Hohenester E]]
[[Category: Jansonius, J N.]]
[[Category: Jansonius JN]]
[[Category: Aminotransferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:55:56 2008''

Latest revision as of 11:39, 1 May 2024

CRYSTALLINE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE EXISTS IN ONLY TWO CONFORMATIONSCRYSTALLINE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE EXISTS IN ONLY TWO CONFORMATIONS

Structural highlights

1tat is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1tat, resolution 3.00Å

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