6np5 | pdb_00006np5

AAC-VIa bound to Kanamycin B

spinqualitylabelsall models 6np5, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6np5 is a 1 chain structure with sequence from "aerobacter_cloacae"_(jordan_1890)_bergey_et_al._1923 "aerobacter cloacae" (jordan 1890) bergey et al. 1923. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 9CS, MG Gene: aac 3-VI ("Aerobacter cloacae" (Jordan 1890) Bergey et al. 1923) Activity: Aminoglycoside N(3')-acetyltransferase, with EC number 2.3.1.81 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The position, bonding and dynamics of hydrogen atoms in the catalytic centers of proteins are essential for catalysis. The role of short hydrogen bonds in catalysis has remained highly debated and led to establishment of several distinctive geometrical arrangements of hydrogen atoms vis-a-vis the heavier donor and acceptor counterparts, that is, low-barrier, single-well or short canonical hydrogen bonds. Here we demonstrate how the position of a hydrogen atom in the catalytic triad of an aminoglycoside inactivating enzyme leads to a thirty-fold increase in catalytic turnover. A low-barrier hydrogen bond is present in the enzyme active site for the substrates that are turned over the best, whereas a canonical hydrogen bond is found with the least preferred substrate. This is the first comparison of these hydrogen bonds involving an identical catalytic network, while directly demonstrating how active site electrostatics adapt to the electronic nature of substrates to tune catalysis. Low-Barrier and Canonical Hydrogen Bonds Modulate Activity and Specificity of a Catalytic Triad.,Kumar P, Agarwal PK, Waddell MB, Mittag T, Serpersu EH, Cuneo MJ Angew Chem Int Ed Engl. 2019 Nov 4;58(45):16260-16266. doi:, 10.1002/anie.201908535. Epub 2019 Sep 24. PMID:31515870 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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