6BBR
Room temperature neutron/X-ray structure of AAC-VIa
Summary for 6BBR
| Entry DOI | 10.2210/pdb6bbr/pdb |
| Related | 6BBZ |
| Descriptor | AAC 3-VI protein, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | acetyltransferase, transferase |
| Biological source | Enterobacter cloacae |
| Total number of polymer chains | 1 |
| Total formula weight | 32368.77 |
| Authors | Cuneo, M.J.,Kumar, P.,Serpersu, E.H. (deposition date: 2017-10-19, release date: 2018-02-28, Last modification date: 2023-10-04) |
| Primary citation | Kumar, P.,Serpersu, E.H.,Cuneo, M.J. A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad. Sci Adv, 4:eaas8667-eaas8667, 2018 Cited by PubMed Abstract: One group of enzymes that confer resistance to aminoglycoside antibiotics through covalent modification belongs to the GCN5-related -acetyltransferase (GNAT) superfamily. We show how a unique GNAT subfamily member uses a previously unidentified noncanonical catalytic triad, consisting of a glutamic acid, a histidine, and the antibiotic substrate itself, which acts as a nucleophile and attacks the acetyl donor molecule. Neutron diffraction studies allow for unambiguous identification of a low-barrier hydrogen bond, predicted in canonical catalytic triads to increase basicity of the histidine. This work highlights the role of this unique catalytic triad in mediating antibiotic resistance while providing new insights into the design of the next generation of aminoglycosides. PubMed: 29632894DOI: 10.1126/sciadv.aas8667 PDB entries with the same primary citation |
| Experimental method | NEUTRON DIFFRACTION (2.3 Å) X-RAY DIFFRACTION (2.002 Å) |
Structure validation
Download full validation report
