3jud

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{{Seed}}
 
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[[Image:3jud.jpg|left|200px]]
 
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==Human gamma-glutamylamine cyclotransferase, E82Q mutant==
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The line below this paragraph, containing "STRUCTURE_3jud", creates the "Structure Box" on the page.
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<StructureSection load='3jud' size='340' side='right'caption='[[3jud]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3jud]] is a 1 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=3JUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JUD FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 0.98&#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=NO3:NITRATE+ION'>NO3</scene></td></tr>
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{{STRUCTURE_3jud| PDB=3jud | SCENE= }}
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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=3jud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jud OCA], [https://pdbe.org/3jud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jud RCSB], [https://www.ebi.ac.uk/pdbsum/3jud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jud ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GGACT_HUMAN GGACT_HUMAN] Contributes to degradation of proteins cross-linked by transglutaminases. Degrades the cross-link between a lysine and a glutamic acid residue from two proteins that have been cross-linked by transglutaminases. Catalyzes the formation of 5-oxoproline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine.<ref>PMID:20110353</ref>
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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/ju/3jud_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=3jud ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Gamma-glutamylamine cyclotransferase (GGACT) is an enzyme that converts gamma-glutamylamines to free amines and 5-oxoproline. GGACT shows high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. The enzyme adopts the newly identified cyclotransferase fold, observed in gamma-glutamylcyclotransferase (GGCT), an enzyme with activity toward gamma-glutamyl-alpha-amino acids (Oakley, A. J., Yamada, T., Liu, D., Coggan, M., Clark, A. G., and Board, P. G. (2008) J. Biol. Chem. 283, 22031-22042). Despite the absence of significant sequence identity, several residues are conserved in the active sites of GGCT and GGACT, including a putative catalytic acid/base residue (GGACT Glu(82)). The structure of GGACT in complex with the reaction product 5-oxoproline provides evidence for a common catalytic mechanism in both enzymes. The proposed mechanism, combined with the three-dimensional structures, also explains the different substrate specificities of these enzymes. Despite significant sequence divergence, there are at least three subfamilies in prokaryotes and eukaryotes that have conserved the GGCT fold and GGCT enzymatic activity.
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===Human gamma-glutamylamine cyclotransferase, E82Q mutant===
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Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism.,Oakley AJ, Coggan M, Board PG J Biol Chem. 2010 Mar 26;285(13):9642-8. Epub 2010 Jan 28. PMID:20110353<ref>PMID:20110353</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20110353}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3jud" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20110353 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20110353}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3JUD is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JUD OCA].
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==Reference==
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<ref group="xtra">PMID:20110353</ref><references group="xtra"/>
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[[Category: Gamma-glutamylcyclotransferase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Oakley, A J.]]
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[[Category: Large Structures]]
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[[Category: 5-oxo-l-proline]]
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[[Category: Oakley AJ]]
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[[Category: Cyclotransferase]]
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[[Category: Cyclotransferase fold]]
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[[Category: Gamma-glutamyl-epsilon-lysine]]
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[[Category: Gamma-glutamylamine cyclotransferase]]
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[[Category: Mutant]]
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[[Category: Oxoproline]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 17:20:40 2010''
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Current revision

Human gamma-glutamylamine cyclotransferase, E82Q mutant

PDB ID 3jud

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