4pa5: Difference between revisions

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== Function ==
== Function ==
[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.
[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.
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== 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<ref>PMID:26322858</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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Latest revision as of 10:19, 1 May 2024

Tgl - a bacterial spore coat transglutaminase - cystamine complexTgl - a bacterial spore coat transglutaminase - cystamine complex

Structural highlights

4pa5 is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.86Å
Ligands:, , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

4pa5, resolution 1.86Å

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OCA
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