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<table cellpadding='5'><tr><td style='background-color: yellow;border:2px solid black;font-size:150%;'> | |||
WARNING: This structure was flagged as problematic. For additional information see '''2014, October:''' at [[Retractions and Fraud]].</td></tr></table> | |||
==Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation== | ==Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation== | ||
<StructureSection load='1l9m' size='340' side='right' caption='[[1l9m]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1l9m' size='340' side='right' caption='[[1l9m]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1l9m]] is a 2 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=1L9M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L9M FirstGlance]. <br> | <table><tr><td colspan='2'>[[1l9m]] is a 2 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=1L9M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L9M FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l9n|1l9n]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l9n|1l9n]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGM3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGM3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
<tr><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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l9m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l9m RCSB], [http://www.ebi.ac.uk/pdbsum/1l9m PDBsum]</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=1l9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l9m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l9m RCSB], [http://www.ebi.ac.uk/pdbsum/1l9m PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
==See Also== | |||
*[[Retractions and Fraud|Retractions and Fraud]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 33: | Line 38: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-glutamine gamma-glutamyltransferase]] | [[Category: Protein-glutamine gamma-glutamyltransferase]] | ||
[[Category: Ahvazi, B | [[Category: Ahvazi, B]] | ||
[[Category: Activation]] | [[Category: Activation]] | ||
[[Category: Calcium binding]] | [[Category: Calcium binding]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Transglutaminase]] | [[Category: Transglutaminase]] | ||
Revision as of 11:15, 18 November 2014
| WARNING: This structure was flagged as problematic. For additional information see 2014, October: at Retractions and Fraud. |
Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activationThree-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
Structural highlights
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 PubMedTransglutaminase (TGase) enzymes catalyze the formation of covalent cross-links between protein-bound glutamines and lysines in a calcium-dependent manner, but the role of Ca(2+) ions remains unclear. The TGase 3 isoform is widely expressed and is important for epithelial barrier formation. It is a zymogen, requiring proteolysis for activity. We have solved the three-dimensional structures of the zymogen and the activated forms at 2.2 and 2.1 A resolution, respectively, and examined the role of Ca(2+) ions. The zymogen binds one ion tightly that cannot be exchanged. Upon proteolysis, the enzyme exothermally acquires two more Ca(2+) ions that activate the enzyme, are exchangeable and are functionally replaceable by other lanthanide trivalent cations. Binding of a Ca(2+) ion at one of these sites opens a channel which exposes the key Trp236 and Trp327 residues that control substrate access to the active site. Together, these biochemical and structural data reveal for the first time in a TGase enzyme that Ca(2+) ions induce structural changes which at least in part dictate activity and, moreover, may confer substrate specificity. Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation.,Ahvazi B, Kim HC, Kee SH, Nemes Z, Steinert PM EMBO J. 2002 May 1;21(9):2055-67. PMID:11980702[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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