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| | <StructureSection load='1iu4' size='340' side='right'caption='[[1iu4]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1iu4' size='340' side='right'caption='[[1iu4]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1iu4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_mobaraensis"_nagatsu_and_suzuki_1963 "streptomyces mobaraensis" nagatsu and suzuki 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IU4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1iu4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_mobaraensis Streptomyces mobaraensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IU4 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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=1iu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iu4 OCA], [http://pdbe.org/1iu4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iu4 RCSB], [http://www.ebi.ac.uk/pdbsum/1iu4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iu4 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=1iu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iu4 OCA], [https://pdbe.org/1iu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iu4 RCSB], [https://www.ebi.ac.uk/pdbsum/1iu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iu4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TGAS_STRMB TGAS_STRMB]] Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. | + | [https://www.uniprot.org/uniprot/TGAS_STRMB TGAS_STRMB] 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: Streptomyces mobaraensis nagatsu and suzuki 1963]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein-glutamine gamma-glutamyltransferase]] | + | [[Category: Streptomyces mobaraensis]] |
| - | [[Category: Ejima, D]] | + | [[Category: Ejima D]] |
| - | [[Category: Ishikawa, K]] | + | [[Category: Ishikawa K]] |
| - | [[Category: Kashiwagi, T]] | + | [[Category: Kashiwagi T]] |
| - | [[Category: Matsui, H]] | + | [[Category: Matsui H]] |
| - | [[Category: Ono, K]] | + | [[Category: Ono K]] |
| - | [[Category: Suzuki, E]] | + | [[Category: Suzuki E]] |
| - | [[Category: Yokoyama, K]] | + | [[Category: Yokoyama K]] |
| - | [[Category: Alpha-beta]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
TGAS_STRMB 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
The crystal structure of a microbial transglutaminase from Streptoverticillium mobaraense has been determined at 2.4 A resolution. The protein folds into a plate-like shape, and has one deep cleft at the edge of the molecule. Its overall structure is completely different from that of the factor XIII-like transglutaminase, which possesses a cysteine protease-like catalytic triad. The catalytic residue, Cys(64), exists at the bottom of the cleft. Asp(255) resides at the position nearest to Cys(64) and is also adjacent to His(274). Interestingly, Cys(64), Asp(255), and His(274) superimpose well on the catalytic triad "Cys-His-Asp" of the factor XIII-like transglutaminase, in this order. The secondary structure frameworks around these residues are also similar to each other. These results imply that both transglutaminases are related by convergent evolution; however, the microbial transglutaminase has developed a novel catalytic mechanism specialized for the cross-linking reaction. The structure accounts well for the catalytic mechanism, in which Asp(255) is considered to be enzymatically essential, as well as for the causes of the higher reaction rate, the broader substrate specificity, and the lower deamidation activity of this enzyme.
Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense.,Kashiwagi T, Yokoyama K, Ishikawa K, Ono K, Ejima D, Matsui H, Suzuki E J Biol Chem. 2002 Nov 15;277(46):44252-60. Epub 2002 Sep 7. PMID:12221081[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kashiwagi T, Yokoyama K, Ishikawa K, Ono K, Ejima D, Matsui H, Suzuki E. Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense. J Biol Chem. 2002 Nov 15;277(46):44252-60. Epub 2002 Sep 7. PMID:12221081 doi:10.1074/jbc.M203933200
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