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| | ==Crystal structure of human transglutaminase 2 complex with adenosine 5' Triphosphate== | | ==Crystal structure of human transglutaminase 2 complex with adenosine 5' Triphosphate== |
| - | <StructureSection load='3ly6' size='340' side='right' caption='[[3ly6]], [[Resolution|resolution]] 3.14Å' scene=''> | + | <StructureSection load='3ly6' size='340' side='right'caption='[[3ly6]], [[Resolution|resolution]] 3.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ly6]] 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=3LY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LY6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ly6]] 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=3LY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LY6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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]] 3.14Å</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=3ly6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ly6 OCA], [https://pdbe.org/3ly6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ly6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ly6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ly6 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=3ly6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ly6 OCA], [http://pdbe.org/3ly6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ly6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ly6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ly6 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. |
| | == 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: Protein-glutamine gamma-glutamyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Han, B G]] | + | [[Category: Han BG]] |
| - | [[Category: Lee, B I]] | + | [[Category: Lee BI]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Diabetes mellitus]]
| + | |
| - | [[Category: Disease mutation]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transglutaminase]]
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| 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
Transglutaminase 2 (TG2) is a calcium-dependent multifunctional protein associated with various human diseases. We determined the crystal structure of human TG2 in complex with adenosine triphosphate (ATP). The ATP molecule binds to the previously identified guanosine diphosphate (GDP) binding pocket but has different hydrogen bonds and ion interaction with protein. The four residues Arg476, Arg478, Val479 and Tyr583, all of which are involved in both ATP and GDP binding by hydrogen bonds, might play important roles in the stabilization of TG2 by ATP or GDP. However, Ser482 and Arg580, which are involved in GDP binding, do not form hydrogen bond with ATP. Additionally, we newly discovered an intramolecular disulfide bond between Cys230 and Cys370, which formation might regulate the enzymatic activity of TG2.
Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate.,Han BG, Cho JW, Cho YD, Jeong KC, Kim SY, Lee BI Int J Biol Macromol. 2010 Aug 1;47(2):190-5. Epub 2010 May 5. PMID:20450932[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Han BG, Cho JW, Cho YD, Jeong KC, Kim SY, Lee BI. Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate. Int J Biol Macromol. 2010 Aug 1;47(2):190-5. Epub 2010 May 5. PMID:20450932 doi:10.1016/j.ijbiomac.2010.04.023
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