4p8i: Difference between revisions

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'''~~Unreleased~~ structure'''

==Tgl - a bacterial spore coat transglutaminase==

== Structural highlights ==

<table><tr><td colspan='2'>[[4p8i]] is a 2 chain structure. 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>

</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>

<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]</span></td></tr>

</table>

== 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.

== 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.

~~The entry 4p8i is ON HOLD until Paper Publication~~

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<ref>PMID:26322858</ref>

~~Authors: Brito~~, J.A.~~, Placido, D~~., ~~Fernandes, C., Lousa, D., Isidro, A., Soares, C.~~M~~., Pohl~~, J., Carrondo, M.A~~., Henriques, A.O., Archer, M.~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description: Tgl -a bacterial spore coat transglutaminase~~

[[Category: ~~Unreleased Structures~~]]

== References ==

[[Category: Henriques, A.O]]

[[Category: ~~Brito~~, J.A]]

__TOC__

</StructureSection>

[[Category: Protein-glutamine gamma-glutamyltransferase]]

[[Category: Archer, M]]

[[Category: Brito, J A]]

[[Category: Carrondo, M A]]

[[Category: Fernandes, C]]

[[Category: Henriques, A O]]

[[Category: Isidro, A]]

[[Category: Lousa, D]]

[[Category: Placido, D]]

~~[[Category: Lousa, D]]~~

[[Category: Pohl, J]]

[[Category: ~~Isidro~~, A]]

[[Category: Soares, C M]]

[[Category: ~~Carrondo, M.A~~]]

[[Category: Bacterial spore coat]]

[[Category: ~~Soares, C.M~~]]

[[Category: Nlpc/p60 endopeptidase]]

[[Category: ~~Archer, M~~]]

[[Category: Papain]]

[[Category: ~~Fernandes, C~~]]

[[Category: Protein cross-linking]]

[[Category: Transferase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Tgl - a bacterial spore coat transglutaminase==
+<StructureSection load='4p8i' size='340' side='right' caption='[[4p8i]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4p8i]] is a 2 chain structure. 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>
+</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>
+<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]</span></td></tr>
+</table>
+== 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.
+<div style="background-color:#fffaf0;">
+== 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.
-The entry 4p8i is ON HOLD  until Paper Publication
+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<ref>PMID:26322858</ref>
-Authors: Brito, J.A., Placido, D., Fernandes, C., Lousa, D., Isidro, A., Soares, C.M., Pohl, J., Carrondo, M.A., Henriques, A.O., Archer, M.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Tgl -a bacterial spore coat transglutaminase
+<div class="pdbe-citations 4p8i" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Henriques, A.O]]
+<references/>
-[[Category: Brito, J.A]]
+__TOC__
+</StructureSection>
+[[Category: Protein-glutamine gamma-glutamyltransferase]]
+[[Category: Archer, M]]
+[[Category: Brito, J A]]
+[[Category: Carrondo, M A]]
+[[Category: Fernandes, C]]
+[[Category: Henriques, A O]]
+[[Category: Isidro, A]]
+[[Category: Lousa, D]]
 [[Category: Placido, D]]
-[[Category: Lousa, D]]
 [[Category: Pohl, J]]
-[[Category: Isidro, A]]
+[[Category: Soares, C M]]
-[[Category: Carrondo, M.A]]
+[[Category: Bacterial spore coat]]
-[[Category: Soares, C.M]]
+[[Category: Nlpc/p60 endopeptidase]]
-[[Category: Archer, M]]
+[[Category: Papain]]
-[[Category: Fernandes, C]]
+[[Category: Protein cross-linking]]
+[[Category: Transferase]]