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{{STRUCTURE_1jg4|  PDB=1jg4  |  SCENE=  }}
===Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with S-adenosylmethionine===
{{ABSTRACT_PUBMED_11700066}}


==Function==
==Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with S-adenosylmethionine==
[[http://www.uniprot.org/uniprot/PIMT_PYRFU PIMT_PYRFU]] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).  
<StructureSection load='1jg4' size='340' side='right'caption='[[1jg4]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1jg4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JG4 FirstGlance]. <br>
[[1jg4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JG4 OCA].  
</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=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jg4 OCA], [https://pdbe.org/1jg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jg4 RCSB], [https://www.ebi.ac.uk/pdbsum/1jg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jg4 ProSAT]</span></td></tr>
<ref group="xtra">PMID:011700066</ref><references group="xtra"/><references/>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PIMT_PYRFU PIMT_PYRFU] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (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/jg/1jg4_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=1jg4 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Boutz, D.]]
[[Category: Boutz D]]
[[Category: Clarke, S.]]
[[Category: Clarke S]]
[[Category: Griffith, S C.]]
[[Category: Griffith SC]]
[[Category: Katz, J.]]
[[Category: Katz J]]
[[Category: Sawaya, M R.]]
[[Category: Sawaya MR]]
[[Category: Thapar, N.]]
[[Category: Thapar N]]
[[Category: Yeates, T O.]]
[[Category: Yeates TO]]
[[Category: Protein repair isomerization]]
[[Category: Rossmann methyltransferase]]
[[Category: Transferase]]

Latest revision as of 07:39, 7 February 2024

Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with S-adenosylmethionine

1jg4, resolution 1.50Å

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