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| | <StructureSection load='2q3z' size='340' side='right'caption='[[2q3z]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2q3z' size='340' side='right'caption='[[2q3z]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2q3z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q3Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2q3z]] 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=2Q3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q3Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=ONL:5-OXO-L-NORLEUCINE'>ONL</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=ONL:5-OXO-L-NORLEUCINE'>ONL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kv3|1kv3]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGM2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [https://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=2q3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3z OCA], [https://pdbe.org/2q3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q3z RCSB], [https://www.ebi.ac.uk/pdbsum/2q3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q3z ProSAT]</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=2q3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3z OCA], [https://pdbe.org/2q3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q3z RCSB], [https://www.ebi.ac.uk/pdbsum/2q3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q3z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein-glutamine gamma-glutamyltransferase]]
| + | [[Category: Brunger AT]] |
| - | [[Category: Brunger, A T]] | + | [[Category: Khosla C]] |
| - | [[Category: Khosla, C]] | + | [[Category: Pinkas DM]] |
| - | [[Category: Pinkas, D M]] | + | [[Category: Strop P]] |
| - | [[Category: Strop, P]] | + | |
| - | [[Category: Tg2]]
| + | |
| - | [[Category: Tissue transglutaminase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transglutaminase 2]]
| + | |
| Structural highlights
Function
TGM2_HUMAN Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Human transglutaminase 2 (TG2), a member of a large family of enzymes that catalyze protein crosslinking, plays an important role in the extracellular matrix biology of many tissues and is implicated in the gluten-induced pathogenesis of celiac sprue. Although vertebrate transglutaminases have been studied extensively, thus far all structurally characterized members of this family have been crystallized in conformations with inaccessible active sites. We have trapped human TG2 in complex with an inhibitor that mimics inflammatory gluten peptide substrates and have solved, at 2-A resolution, its x-ray crystal structure. The inhibitor stabilizes TG2 in an extended conformation that is dramatically different from earlier transglutaminase structures. The active site is exposed, revealing that catalysis takes place in a tunnel, bridged by two tryptophan residues that separate acyl-donor from acyl-acceptor and stabilize the tetrahedral reaction intermediates. Site-directed mutagenesis was used to investigate the acyl-acceptor side of the tunnel, yielding mutants with a marked increase in preference for hydrolysis over transamidation. By providing the ability to visualize this activated conformer, our results create a foundation for understanding the catalytic as well as the non-catalytic roles of TG2 in biology, and for dissecting the process by which the autoantibody response to TG2 is induced in celiac sprue patients.
Transglutaminase 2 undergoes a large conformational change upon activation.,Pinkas DM, Strop P, Brunger AT, Khosla C PLoS Biol. 2007 Dec;5(12):e327. PMID:18092889[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pinkas DM, Strop P, Brunger AT, Khosla C. Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol. 2007 Dec;5(12):e327. PMID:18092889 doi:http://dx.doi.org/10.1371/journal.pbio.0050327
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