6bc4

Cryo X-ray structure of acetyl coenzyme A bound AAC-VIa

spinqualitylabelsall models 6bc4, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6bc4 is a 1 chain structure with sequence from Enterobacter cloacae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.049Å Ligands: ACO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q47030_ENTCL Publication Abstract from PubMed One group of enzymes that confer resistance to aminoglycoside antibiotics through covalent modification belongs to the GCN5-related N-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. A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad.,Kumar P, Serpersu EH, Cuneo MJ Sci Adv. 2018 Apr 4;4(4):eaas8667. doi: 10.1126/sciadv.aas8667. eCollection 2018 , Apr. PMID:29632894 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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