Structural and Enzymatic Characterization of a Nucleoside Diphosphate Sugar Hydrolase from Bdellovibrio bacteriovorus

de la Peña, Andres H.; Suarez, Allison; Duong-ly, Krisna C.; Schoeffield, Andrew J.; Pizarro-Dupuy, Mario A.; Zarr, Melissa; Pineiro, Silvia A.; Amzel, L. Mario; Gabelli, Sandra B.

doi:10.1371/journal.pone.0141716

Structural and Enzymatic Characterization of a Nucleoside Diphosphate Sugar Hydrolase from Bdellovibrio bacteriovorus

Journal Article · Sun Nov 01 23:00:00 EST 2015 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0141716· OSTI ID:1627768

de la Peña, Andres H. ^[1]; Suarez, Allison ^[2]; Duong-ly, Krisna C. ^[2]; Schoeffield, Andrew J. ^[3]; Pizarro-Dupuy, Mario A. ^[2]; Zarr, Melissa ^[2]; Pineiro, Silvia A. ^[4]; Amzel, L. Mario ^[2]; Gabelli, Sandra B. ^[2]

Johns Hopkins Univ., Baltimore, MD (United States). School of Medicine; DOE/OSTI
Johns Hopkins Univ., Baltimore, MD (United States). School of Medicine
Loyola University, Baltimore, MD (United States)
Univ. of Maryland, Baltimore, MD (United States); U.S. Food and Drug Administration (FDA), Rockville, MD (United States)

Given the broad range of substrates hydrolyzed by Nudix (nucleoside diphosphate linked to X) enzymes, identification of sequence and structural elements that correctly predict a Nudix substrate or characterize a family is key to correctly annotate the myriad of Nudix enzymes. Here, we present the structure determination and characterization of Bd3179 –- a Nudix hydrolase from Bdellovibrio bacteriovorus–that we show localized in the periplasmic space of this obligate Gram-negative predator. We demonstrate that the enzyme is a nucleoside diphosphate sugar hydrolase (NDPSase) and has a high degree of sequence and structural similarity to a canonical ADP-ribose hydrolase and to a nucleoside diphosphate sugar hydrolase (1.4 and 1.3 Å Cα RMSD respectively). Examination of the structural elements conserved in both types of enzymes confirms that an aspartate-X-lysine motif on the C-terminal helix of the α-β-α NDPSase fold differentiates NDPSases from ADPRases.

View Accepted Manuscript (DOE)

Research Organization:: Brookhaven National Lab., Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC); Stewart Trust Fellowship; National Science Foundation (NSF); National Institutes of Health (NIH)

Grant/Contract Number:: SC0012704; AC02-98CH10886

OSTI ID:: 1627768

Journal Information:: PLoS ONE, Journal Name: PLoS ONE Journal Issue: 11 Vol. 10; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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