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| | ==Tgl - a bacterial spore coat transglutaminase== | | ==Tgl - a bacterial spore coat transglutaminase== |
| - | <StructureSection load='4p8i' size='340' side='right' caption='[[4p8i]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='4p8i' size='340' side='right'caption='[[4p8i]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p8i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P8I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P8I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4p8i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P8I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P8I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tgl, yugV, yuxF, BSU31270 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=4p8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p8i OCA], [https://pdbe.org/4p8i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p8i RCSB], [https://www.ebi.ac.uk/pdbsum/4p8i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p8i ProSAT]</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 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=4p8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p8i OCA], [http://pdbe.org/4p8i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p8i RCSB], [http://www.ebi.ac.uk/pdbsum/4p8i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p8i ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TGL_BACSU TGL_BACSU]] Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. In wild-type spores at 37 degrees Celsius, tgl mediates the cross-linking of GerQ in higher molecular mass forms, probably in cooperation with YabG. | + | [https://www.uniprot.org/uniprot/TGL_BACSU TGL_BACSU] Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. In wild-type spores at 37 degrees Celsius, tgl mediates the cross-linking of GerQ in higher molecular mass forms, probably in cooperation with YabG. |
| | <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: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Protein-glutamine gamma-glutamyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Archer, M]] | + | [[Category: Archer M]] |
| - | [[Category: Brito, J A]] | + | [[Category: Brito JA]] |
| - | [[Category: Carrondo, M A]] | + | [[Category: Carrondo MA]] |
| - | [[Category: Fernandes, C]] | + | [[Category: Fernandes C]] |
| - | [[Category: Henriques, A O]] | + | [[Category: Henriques AO]] |
| - | [[Category: Isidro, A]] | + | [[Category: Isidro A]] |
| - | [[Category: Lousa, D]] | + | [[Category: Lousa D]] |
| - | [[Category: Placido, D]] | + | [[Category: Placido D]] |
| - | [[Category: Pohl, J]] | + | [[Category: Pohl J]] |
| - | [[Category: Soares, C M]] | + | [[Category: Soares CM]] |
| - | [[Category: Bacterial spore coat]]
| + | |
| - | [[Category: Nlpc/p60 endopeptidase]]
| + | |
| - | [[Category: Papain]]
| + | |
| - | [[Category: Protein cross-linking]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
TGL_BACSU Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. In wild-type spores at 37 degrees Celsius, tgl mediates the cross-linking of GerQ in higher molecular mass forms, probably in cooperation with YabG.
Publication Abstract from PubMed
Transglutaminases are best known for their ability to catalyze protein cross-linking reactions that impart chemical and physical resilience to cellular structures. Here, we report the crystal structure and characterization of Tgl, a transglutaminase from the bacterium Bacillus subtilis. Tgl is produced during sporulation and cross-links the surface of the highly resilient spore. Tgl-like proteins are found only in spore-forming bacteria of the Bacillus and Clostridia classes, indicating an ancient origin. Tgl is a single-domain protein, produced in active form, and the smallest transglutaminase characterized to date. We show that Tgl is structurally similar to bacterial cell wall endopeptidases and has an NlpC/P60 catalytic core, thought to represent the ancestral unit of the cysteine protease fold. We show that Tgl functions through a unique partially redundant catalytic dyad formed by Cys116 and Glu187 or Glu115. Strikingly, the catalytic Cys is insulated within a hydrophobic tunnel that traverses the molecule from side to side. The lack of similarity of Tgl to other transglutaminases together with its small size suggests that an NlpC/P60 catalytic core and insulation of the active site during catalysis may be essential requirements for protein cross-linking.
Structural and Functional Characterization of an Ancient Bacterial Transglutaminase Sheds Light on the Minimal Requirements for Protein Cross-Linking.,Fernandes CG, Placido D, Lousa D, Brito JA, Isidro A, Soares CM, Pohl J, Carrondo MA, Archer M, Henriques AO Biochemistry. 2015 Sep 22;54(37):5723-34. doi: 10.1021/acs.biochem.5b00661. Epub , 2015 Sep 8. PMID:26322858[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fernandes CG, Placido D, Lousa D, Brito JA, Isidro A, Soares CM, Pohl J, Carrondo MA, Archer M, Henriques AO. Structural and Functional Characterization of an Ancient Bacterial Transglutaminase Sheds Light on the Minimal Requirements for Protein Cross-Linking. Biochemistry. 2015 Sep 22;54(37):5723-34. doi: 10.1021/acs.biochem.5b00661. Epub , 2015 Sep 8. PMID:26322858 doi:http://dx.doi.org/10.1021/acs.biochem.5b00661
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