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| | ==Transglutaminase 2 mutant G224V in complex with GTP== | | ==Transglutaminase 2 mutant G224V in complex with GTP== |
| - | <StructureSection load='6a8p' size='340' side='right' caption='[[6a8p]], [[Resolution|resolution]] 2.54Å' scene=''> | + | <StructureSection load='6a8p' size='340' side='right'caption='[[6a8p]], [[Resolution|resolution]] 2.54Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6a8p]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A8P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6a8p]] is a 3 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=6A8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A8P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.537Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13] </span></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=6a8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8p OCA], [https://pdbe.org/6a8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a8p RCSB], [https://www.ebi.ac.uk/pdbsum/6a8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8p ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6a8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8p OCA], [http://pdbe.org/6a8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a8p RCSB], [http://www.ebi.ac.uk/pdbsum/6a8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TGM2_HUMAN TGM2_HUMAN]] Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. | + | [https://www.uniprot.org/uniprot/TGM2_HUMAN TGM2_HUMAN] Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Protein-glutamine gamma-glutamyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Ha, H J]] | + | [[Category: Ha HJ]] |
| - | [[Category: Kwon, S]] | + | [[Category: Kwon S]] |
| - | [[Category: Park, H H]] | + | [[Category: Park HH]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Gtp]]
| + | |
| - | [[Category: Mutant]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transglutaminase]]
| + | |
| Structural highlights
Function
TGM2_HUMAN Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
Publication Abstract from PubMed
Multi-functional transglutaminase 2 (TG2), which possesses protein cross-linking and GTP hydrolysis activities, is involved in various cellular processes, including apoptosis, angiogenesis, wound healing, and neuronal regeneration, and is associated with many human diseases, including inflammatory disease, celiac disease, neurodegenerative disease, diabetes, tissue fibrosis, and cancers. Although most biochemical and cellular studies have been conducted with the TG2 (G224) form, the TG2 (G224V) form has recently emerged as a putative natural variant of TG2. In this study, we characterized the putative natural form of TG2, TG2 (G224V), and through a new crystal structure of TG2 (G224V), we revealed how TG2 (G224V) gained stability and higher Ca2+-dependent activity than an artificial variant of TG2 (G224).
Structure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity.,Ha HJ, Kwon S, Jeong EM, Kim CM, Lee KB, Kim IG, Park HH PLoS One. 2018 Oct 15;13(10):e0204707. doi: 10.1371/journal.pone.0204707., eCollection 2018. PMID:30321187[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ha HJ, Kwon S, Jeong EM, Kim CM, Lee KB, Kim IG, Park HH. Structure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity. PLoS One. 2018 Oct 15;13(10):e0204707. doi: 10.1371/journal.pone.0204707., eCollection 2018. PMID:30321187 doi:http://dx.doi.org/10.1371/journal.pone.0204707
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