1dju: Difference between revisions

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[[Image:1dju.jpg|left|200px]]


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==CRYSTAL STRUCTURE OF AROMATIC AMINOTRANSFERASE FROM PYROCOCCUS HORIKOSHII OT3==
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<StructureSection load='1dju' size='340' side='right'caption='[[1dju]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1dju]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DJU FirstGlance]. <br>
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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]] 2.1&#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_1dju|  PDB=1dju  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dju OCA], [https://pdbe.org/1dju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dju RCSB], [https://www.ebi.ac.uk/pdbsum/1dju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dju ProSAT]</span></td></tr>
 
</table>
'''CRYSTAL STRUCTURE OF AROMATIC AMINOTRANSFERASE FROM PYROCOCCUS HORIKOSHII OT3'''
== Function ==
 
[https://www.uniprot.org/uniprot/O59096_PYRHO O59096_PYRHO]
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
Aromatic amino acid aminotransferase (ArATPh), which has a melting temperature of 120 degrees C, is one of the most thermostable aminotransferases yet to be discovered. The crystal structure of this aminotransferase from the hyperthermophilic archaeon Pyrococcus horikoshii was determined to a resolution of 2.1 A. ArATPh has a homodimer structure in which each subunit is composed of two domains, in a manner similar to other well characterized aminotransferases. By the least square fit after superposing on a mesophilic ArAT, the ArATPh molecule exhibits a large deviation of the main chain coordinates, three shortened alpha-helices, an elongated loop connecting two domains, and a long loop transformed from an alpha-helix, which are all factors that are likely to contribute to its hyperthermostability. The pyridine ring of the cofactor pyridoxal 5'-phosphate covalently binding to Lys(233) is stacked parallel to F121 on one side and interacts with the geminal dimethyl-CH/pi groups of Val(201) on the other side. This tight stacking against the pyridine ring probably contributes to the hyperthermostability of ArATPh. Compared with other ArATs, ArATPh has a novel substrate specificity, the order of preference being Tyr &gt; Phe &gt; Glu &gt; Trp &gt; His&gt;&gt; Met &gt; Leu &gt; Asp &gt; Asn. Its relatively weak activity against Asp is due to lack of an arginine residue corresponding to Arg(292)* (where the asterisk indicates that this is a residues supplied by the other subunit of the dimer) in pig cytosolic aspartate aminotransferase. The enzyme recognizes the aromatic substrate by hydrophobic interaction with aromatic rings (Phe(121) and Tyr(59)*) and probably recognizes acidic substrates by a hydrophilic interaction involving a hydrogen bond network with Thr(264)*.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dj/1dju_consurf.spt"</scriptWhenChecked>
1DJU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJU OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
The molecular structure of hyperthermostable aromatic aminotransferase with novel substrate specificity from Pyrococcus horikoshii., Matsui I, Matsui E, Sakai Y, Kikuchi H, Kawarabayasi Y, Ura H, Kawaguchi S, Kuramitsu S, Harata K, J Biol Chem. 2000 Feb 18;275(7):4871-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10671523 10671523]
</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=1dju ConSurf].
[[Category: Pyrococcus horikoshii]]
<div style="clear:both"></div>
[[Category: Single protein]]
__TOC__
[[Category: Kawarabayashi, H.]]
</StructureSection>
[[Category: Kikuchi, H.]]
[[Category: Large Structures]]
[[Category: Matsui, E.]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Matsui, I.]]
[[Category: Kawarabayashi H]]
[[Category: Sakai, Y.]]
[[Category: Kikuchi H]]
[[Category: Alpha/beta/alpha]]
[[Category: Matsui E]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:55:54 2008''
[[Category: Matsui I]]
[[Category: Sakai Y]]

Latest revision as of 12:51, 20 March 2024

CRYSTAL STRUCTURE OF AROMATIC AMINOTRANSFERASE FROM PYROCOCCUS HORIKOSHII OT3CRYSTAL STRUCTURE OF AROMATIC AMINOTRANSFERASE FROM PYROCOCCUS HORIKOSHII OT3

Structural highlights

1dju is a 2 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O59096_PYRHO

Evolutionary Conservation

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

1dju, resolution 2.10Å

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