Crystal structure of a polyglycine hydrolase determined using a RoseTTAFold model

The objective of this research was to investigate the proteolytic mechanism and other characteristics by structural and biochemical means. Here, the first atomic structure of a polyglycine hydrolase was identified. It was solved by X-ray crystallography using a RoseTTAFold model, taking advantage of recent technical advances in structure prediction. PGHs are composed of two domains: the N- and C-domains. The N-domain is a novel tertiary fold with an as-yet unknown function that is found across all kingdoms of life. The C-domain shares structural similarities with class C β -lactamases, including a common catalytic nucleophilic serine. In addition to insights into the PGH family and its relationship to β -lactamases, the results demonstrate the power of complementing experimental structure determination with new computational techniques.

Source: Acta Crystallographica Section D - February 6, 2023 Category: Biochemistry Authors: Dowling, N.V. Naumann, T.A. Price, N.P.J. Rose, D.R. Tags: RoseTTAFold fungi chitinase-modifying proteins polyglycine hydrolases β -lactamases research papers Source Type: research