1jg3

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(New page: 200px<br /><applet load="1jg3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jg3, resolution 2.1&Aring;" /> '''Crystal Structure of ...)
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[[Image:1jg3.jpg|left|200px]]<br /><applet load="1jg3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jg3, resolution 2.1&Aring;" />
 
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'''Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with adenosine & VYP(ISP)HA substrate'''<br />
 
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==Overview==
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==Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with adenosine & VYP(ISP)HA substrate==
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Protein L-isoaspartyl (D-aspartyl) methyltransferases (EC 2.1.1.77) are, found in almost all organisms. These enzymes catalyze the, S-adenosylmethionine (AdoMet)-dependent methylation of isomerized and, racemized aspartyl residues in age-damaged proteins as part of an, essential protein repair process. Here, we report crystal structures of, the repair methyltransferase at resolutions up to 1.2 A from the, hyperthermophilic archaeon Pyrococcus furiosus. Refined structures include, binary complexes with the active cofactor AdoMet, its reaction product, S-adenosylhomocysteine (AdoHcy), and adenosine. The enzyme places the, methyl-donating cofactor in a deep, electrostatically negative pocket that, is shielded from solvent. Across the multiple crystal structures, visualized, the presence or absence of the methyl group on the cofactor, correlates with a significant conformational change in the enzyme in a, loop bordering the active site, suggesting a role for motion in catalysis, or cofactor exchange. We also report the structure of a ternary complex of, the enzyme with adenosine and the methyl-accepting polypeptide substrate, VYP(L-isoAsp)HA at 2.1 A. The substrate binds in a narrow active site, cleft with three of its residues in an extended conformation, suggesting, that damaged proteins may be locally denatured during the repair process, in cells. Manual and computer-based docking studies on different isomers, help explain how the enzyme uses steric effects to make the critical, distinction between normal L-aspartyl and age-damaged L-isoaspartyl and, D-aspartyl residues.
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<StructureSection load='1jg3' size='340' side='right'caption='[[1jg3]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1jg3]] is a 4 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=1JG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JG3 FirstGlance]. <br>
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1JG3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with CL, NA and ADN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JG3 OCA].
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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=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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==Reference==
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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=1jg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jg3 OCA], [https://pdbe.org/1jg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jg3 RCSB], [https://www.ebi.ac.uk/pdbsum/1jg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jg3 ProSAT]</span></td></tr>
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Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate., Griffith SC, Sawaya MR, Boutz DR, Thapar N, Katz JE, Clarke S, Yeates TO, J Mol Biol. 2001 Nov 9;313(5):1103-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11700066 11700066]
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</table>
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[[Category: Protein-L-isoaspartate(D-aspartate) O-methyltransferase]]
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== Function ==
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[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).
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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/jg/1jg3_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=1jg3 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
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[[Category: Single protein]]
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[[Category: Boutz D]]
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[[Category: Boutz, D.]]
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[[Category: Clarke S]]
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[[Category: Clarke, S.]]
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[[Category: Griffith SC]]
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[[Category: Griffith, S.C.]]
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[[Category: Katz J]]
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[[Category: Katz, J.]]
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[[Category: Sawaya MR]]
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[[Category: Sawaya, M.R.]]
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[[Category: Thapar N]]
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[[Category: Thapar, N.]]
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[[Category: Yeates TO]]
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[[Category: Yeates, T.O.]]
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[[Category: ADN]]
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[[Category: CL]]
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[[Category: NA]]
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[[Category: protein repair isomerization]]
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[[Category: rossmann methyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:12:56 2007''
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Current revision

Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with adenosine & VYP(ISP)HA substrate

PDB ID 1jg3

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