6TAF
Bd0314 DslA E154Q mutant
Summary for 6TAF
| Entry DOI | 10.2210/pdb6taf/pdb |
| Related | 6TA9 6TAB 6TAD |
| Descriptor | SLT domain-containing protein, SULFATE ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | lysozyme peptidoglycan, hydrolase |
| Biological source | Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) |
| Total number of polymer chains | 1 |
| Total formula weight | 28339.73 |
| Authors | Lovering, A.L.,Harding, C.J. (deposition date: 2019-10-29, release date: 2020-07-15, Last modification date: 2024-10-23) |
| Primary citation | Harding, C.J.,Huwiler, S.G.,Somers, H.,Lambert, C.,Ray, L.J.,Till, R.,Taylor, G.,Moynihan, P.J.,Sockett, R.E.,Lovering, A.L. A lysozyme with altered substrate specificity facilitates prey cell exit by the periplasmic predator Bdellovibrio bacteriovorus. Nat Commun, 11:4817-4817, 2020 Cited by PubMed Abstract: Lysozymes are among the best-characterized enzymes, acting upon the cell wall substrate peptidoglycan. Here, examining the invasive bacterial periplasmic predator Bdellovibrio bacteriovorus, we report a diversified lysozyme, DslA, which acts, unusually, upon (GlcNAc-) deacetylated peptidoglycan. B. bacteriovorus are known to deacetylate the peptidoglycan of the prey bacterium, generating an important chemical difference between prey and self walls and implying usage of a putative deacetyl-specific "exit enzyme". DslA performs this role, and ΔDslA strains exhibit a delay in leaving from prey. The structure of DslA reveals a modified lysozyme superfamily fold, with several adaptations. Biochemical assays confirm DslA specificity for deacetylated cell wall, and usage of two glutamate residues for catalysis. Exogenous DslA, added ex vivo, is able to prematurely liberate B. bacteriovorus from prey, part-way through the predatory lifecycle. We define a mechanism for specificity that invokes steric selection, and use the resultant motif to identify wider DslA homologues. PubMed: 32968056DOI: 10.1038/s41467-020-18139-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.336 Å) |
Structure validation
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