A new structural arrangement in proteins involving lysine NH₃⁺ group and carbonyl.

ABSTRACT: Screening of the Protein Data Bank led to identification of a recurring structural motif where lysine NH₃⁺ group interacts with backbone carbonyl. This interaction is characterized by linear atom arrangement, with carbonyl O atom positioned on the three-fold symmetry axis of the NH₃⁺ group (angle C^ε-N^ζ-O close to 180°, distance N^ζ-O ca. 2.7-3.0 Å). Typically, this linear arrangement coexists with three regular hydrogen bonds formed by lysine NH₃⁺ group (angle C^ε-N^ζ-acceptor atom close to 109°, distance N^ζ-acceptor atom ca. 2.7-3.0 Å). Our DFT calculations using polarizable continuum environment suggest that this newly identified linear interaction makes an app

SUBMITTER: Rogacheva ON 

PROVIDER: S-EPMC5704018 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature