4de4 | pdb_00004de4

Crystal structure of aminoglycoside phosphotransferase APH(2")-Id/APH(2")-IVa in complex with HEPES

spinqualitylabelsall models 4de4, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4de4 is a 2 chain structure with sequence from "streptococcus_casseliflavus"_vaughan_et_al._1979 "streptococcus casseliflavus" vaughan et al. 1979. This structure supersedes the now removed PDB entry 3r80. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EPE NonStd Res: MSE Related: 3r7z, 3r81, 3r82 Gene: aph(2")-Id ("Streptococcus casseliflavus" Vaughan et al. 1979) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Kinase-mediated resistance to antibiotics is a significant clinical challenge. These enzymes share a common protein fold characteristic of Ser/Thr/Tyr protein kinases. We screened 14 antibiotic resistance kinases against 80 chemically diverse protein kinase inhibitors to map resistance kinase chemical space. The screens identified molecules with both broad and narrow inhibition profiles, proving that protein kinase inhibitors offer privileged chemical matter with the potential to block antibiotic resistance. One example is the flavonol quercetin, which inhibited a number of resistance kinases in vitro and in vivo. This activity was rationalized by determination of the crystal structure of the aminoglycoside kinase APH(2)-IVa in complex with quercetin and its antibiotic substrate kanamycin. Our data demonstrate that protein kinase inhibitors offer chemical scaffolds that can block antibiotic resistance, providing leads for co-drug design. A small molecule discrimination map of the antibiotic resistance kinome.,Shakya T, Stogios PJ, Waglechner N, Evdokimova E, Ejim L, Blanchard JE, McArthur AG, Savchenko A, Wright GD Chem Biol. 2011 Dec 23;18(12):1591-601. PMID:22195561 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphotransferase

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