4L1G
Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus
Summary for 4L1G
| Entry DOI | 10.2210/pdb4l1g/pdb |
| Descriptor | Peptidoglycan N-acetylglucosamine deacetylase, SULFATE ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | tim barrel, hydrolase, polysaccharide deacetylase |
| Biological source | Bacillus cereus |
| Total number of polymer chains | 4 |
| Total formula weight | 126605.78 |
| Authors | Tsalafouta, A.,Fadouloglou, V.E.,Kokkinidis, M. (deposition date: 2013-06-03, release date: 2014-06-04, Last modification date: 2023-12-06) |
| Primary citation | Fadouloglou, V.E.,Balomenou, S.,Aivaliotis, M.,Kotsifaki, D.,Arnaouteli, S.,Tomatsidou, A.,Efstathiou, G.,Kountourakis, N.,Miliara, S.,Griniezaki, M.,Tsalafouta, A.,Pergantis, S.A.,Boneca, I.G.,Glykos, N.M.,Bouriotis, V.,Kokkinidis, M. Unusual alpha-Carbon Hydroxylation of Proline Promotes Active-Site Maturation. J.Am.Chem.Soc., 139:5330-5337, 2017 Cited by PubMed Abstract: The full extent of proline (Pro) hydroxylation has yet to be established, as it is largely unexplored in bacteria. We describe here a so far unknown Pro hydroxylation activity which occurs in active sites of polysaccharide deacetylases (PDAs) from bacterial pathogens, modifying the protein backbone at the C atom of a Pro residue to produce 2-hydroxyproline (2-Hyp). This process modifies with high specificity a conserved Pro, shares with the deacetylation reaction the same active site and one catalytic residue, and utilizes molecular oxygen as source for the hydroxyl group oxygen of 2-Hyp. By providing additional hydrogen-bonding capacity, the Pro→2-Hyp conversion alters the active site and enhances significantly deacetylase activity, probably by creating a more favorable environment for transition-state stabilization. Our results classify this process as an active-site "maturation", which is highly atypical in being a protein backbone-modifying activity, rather than a side-chain-modifying one. PubMed: 28333455DOI: 10.1021/jacs.6b12209 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.336 Å) |
Structure validation
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