6gmg | pdb_00006gmg

Structure of a glutamine donor mimicking inhibitory peptide shaped by the catalytic cleft of microbial transglutaminase

spinqualitylabelsall models 6gmg, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6gmg is a 4 chain structure with sequence from Streptomyces mobaraensis and Streptomyces mobaraensis NBRC 13819 = DSM 40847. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: FLC, OAS, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAPI_STRMB Stress protein produced under hyperthermal stress conditions. Serves as a glutamine and lysine donor substrate for transglutaminase. Inhibits the cysteine proteases papain and bromelain as well as the bovine serine protease trypsin. Has hardly any or no effect on subtilisin, bovine chymotrypsin, proteinase K from T.album, transglutaminase-activating metalloproteinase (TAMEP) from S.mobaraensis, dispase from B.polymyxa, thermolysin from B.thermoproteolyticus or collagenase from C.histolyticum. Publication Abstract from PubMed The protein cross-linking enzyme transglutaminase from Streptomyces mobaraensis (MTG) is frequently used to modify therapeutic proteins. In order to reveal the binding mode of glutamine donor substrates, we have now crystallized MTG covalently linked to large inhibitory peptides. A series of peptide structures were examined but DIPIGSKMTG, which was chloroacetylated at serine, was the only inhibitory molecule that resulted in an interpretable density map. We found that, besides the warhead (modified Ser6), Ile4 and Gly5 of the inhibitory peptide occupy the tight but extended hydrophobic bottom of the MTG binding cleft. Both termini of the peptide protrude along the cleft walls almost perpendicular to the bottom of the extended cleft. This peptide model suggests a zipper-like cross-linking mechanism of self-assembled substrate proteins by MTG. This article is protected by copyright. All rights reserved. Structure of a glutamine donor mimicking inhibitory peptide shaped by the catalytic cleft of microbial transglutaminase.,Juettner NE, Schmelz S, Kraemer A, Knapp S, Becker B, Kolmar H, Scrima A, Fuchsbauer HL FEBS J. 2018 Oct 15. doi: 10.1111/febs.14678. PMID:30318745 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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