1fj2: Difference between revisions

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New page: left|200px<br /> <applet load="1fj2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fj2, resolution 1.5Å" /> '''Crystal structure of...
 
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[[Image:1fj2.gif|left|200px]]<br />
<applet load="1fj2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fj2, resolution 1.5&Aring;" />
'''Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution'''<br />


==Overview==
==Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution==
BACKGROUND: Many proteins undergo posttranslational modifications, involving covalent attachment of lipid groups. Among them is, palmitoylation, a dynamic, reversible process that affects trimeric G, proteins and Ras and constitutes a regulatory mechanism for signal, transduction pathways. Recently, an acylhydrolase previously identified as, lysophospholipase has been shown to function as an acyl protein, thioesterase, which catalyzes depalmitoylation of Galpha proteins as well, as Ras. Its amino acid sequence suggested that the protein is, evolutionarily related to neutral lipases and other thioesterases, but, direct structural information was not available. RESULTS: We have solved, the crystal structure of the human putative Galpha-regulatory protein acyl, thioesterase (hAPT1) with a ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11080636 (full description)]]
<StructureSection load='1fj2' size='340' side='right'caption='[[1fj2]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fj2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FJ2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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=1fj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fj2 OCA], [https://pdbe.org/1fj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fj2 RCSB], [https://www.ebi.ac.uk/pdbsum/1fj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fj2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYPA1_HUMAN LYPA1_HUMAN] Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity and also low lysophospholipase activity.<ref>PMID:20418879</ref>
== 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/fj/1fj2_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=1fj2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FJ2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with BR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.39 3.1.4.39]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FJ2 OCA]].
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A., Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS, Structure. 2000 Nov 15;8(11):1137-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11080636 11080636]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dauter, Z.]]
[[Category: Dauter Z]]
[[Category: Derewenda, Z.]]
[[Category: Derewenda Z]]
[[Category: Devedjiev, Y.]]
[[Category: Devedjiev Y]]
[[Category: Jones, T.]]
[[Category: Jones T]]
[[Category: Kuznetsov, S.]]
[[Category: Kuznetsov S]]
[[Category: BR]]
[[Category: alpha/beta hydrolase]]
[[Category: anomalous diffraction]]
[[Category: sad]]
[[Category: serine hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:30:18 2007''

Latest revision as of 07:14, 7 February 2024

Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution

1fj2, resolution 1.50Å

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