Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus
Abstract
When exposed to high osmolarity, methicillin-resistant Staphylococcus aureus (MRSA) restores its growth and establishes a new steady state by accumulating the osmoprotectant metabolite betaine. Effective osmoregulation has also been implicated in the acquirement of a profound antibiotic resistance by MRSA. Betaine can be obtained from the bacterial habitat or produced intracellularly from choline via the toxic betaine aldehyde (BA) employing the choline dehydrogenase and betaine aldehyde dehydrogenase (BADH) enzymes. Here, it is shown that the putative betaine aldehyde dehydrogenase SACOL2628 from the early MRSA isolate COL ( SaBADH) utilizes betaine aldehyde as the primary substrate and nicotinamide adenine dinucleotide (NAD+) as the cofactor. Surface plasmon resonance experiments revealed that the affinity of NAD+, NADH and BA for SaBADH is affected by temperature, pH and buffer composition. Finally, five crystal structures of the wild type and three structures of the Gly234Ser mutant of SaBADH in the apo and holo forms provide details of the molecular mechanisms of activity and substrate specificity/inhibition of this enzyme.
- Authors:
-
- Northwestern Univ., Chicago, IL (United States). Dept. of Biochemistry and Molecular Genetics; Center for Structural Genomics of Infectious Diseases (CSGID), Chicago, IL (United States)
- Biosensor Tools LLC, Salt Lake City, UT (United States)
- Univ. of Toronto, ON (Canada). Dept. of Chemical Engineering and Applied Chemistry
- Center for Structural Genomics of Infectious Diseases (CSGID), Chicago, IL (United States)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1233329
- Grant/Contract Number:
- AC02-06CH11357; 085P1000817; HHSN272200700058C; HHSN272201200026C
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Acta Crystallographica. Section D: Biological Crystallography (Online)
- Additional Journal Information:
- Journal Name: Acta Crystallographica. Section D: Biological Crystallography (Online); Journal Volume: 71; Journal Issue: 5; Journal ID: ISSN 1399-0047
- Publisher:
- International Union of Crystallography
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; betaine aldehyde dehydrogenase; Staphylococcus aureus; structural genomics; high-throughput approach; infectious diseases
Citation Formats
Halavaty, Andrei S., Rich, Rebecca L., Chen, Chao, Joo, Jeong Chan, Minasov, George, Dubrovska, Ievgeniia, Winsor, James R., Myszka, David G., Duban, Mark, Shuvalova, Ludmilla, Yakunin, Alexander F., and Anderson, Wayne F. Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus. United States: N. p., 2015.
Web. doi:10.1107/S1399004715004228.
Halavaty, Andrei S., Rich, Rebecca L., Chen, Chao, Joo, Jeong Chan, Minasov, George, Dubrovska, Ievgeniia, Winsor, James R., Myszka, David G., Duban, Mark, Shuvalova, Ludmilla, Yakunin, Alexander F., & Anderson, Wayne F. Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus. United States. https://doi.org/10.1107/S1399004715004228
Halavaty, Andrei S., Rich, Rebecca L., Chen, Chao, Joo, Jeong Chan, Minasov, George, Dubrovska, Ievgeniia, Winsor, James R., Myszka, David G., Duban, Mark, Shuvalova, Ludmilla, Yakunin, Alexander F., and Anderson, Wayne F. Sat .
"Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus". United States. https://doi.org/10.1107/S1399004715004228. https://www.osti.gov/servlets/purl/1233329.
@article{osti_1233329,
title = {Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus},
author = {Halavaty, Andrei S. and Rich, Rebecca L. and Chen, Chao and Joo, Jeong Chan and Minasov, George and Dubrovska, Ievgeniia and Winsor, James R. and Myszka, David G. and Duban, Mark and Shuvalova, Ludmilla and Yakunin, Alexander F. and Anderson, Wayne F.},
abstractNote = {When exposed to high osmolarity, methicillin-resistant Staphylococcus aureus (MRSA) restores its growth and establishes a new steady state by accumulating the osmoprotectant metabolite betaine. Effective osmoregulation has also been implicated in the acquirement of a profound antibiotic resistance by MRSA. Betaine can be obtained from the bacterial habitat or produced intracellularly from choline via the toxic betaine aldehyde (BA) employing the choline dehydrogenase and betaine aldehyde dehydrogenase (BADH) enzymes. Here, it is shown that the putative betaine aldehyde dehydrogenase SACOL2628 from the early MRSA isolate COL ( SaBADH) utilizes betaine aldehyde as the primary substrate and nicotinamide adenine dinucleotide (NAD+) as the cofactor. Surface plasmon resonance experiments revealed that the affinity of NAD+, NADH and BA for SaBADH is affected by temperature, pH and buffer composition. Finally, five crystal structures of the wild type and three structures of the Gly234Ser mutant of SaBADH in the apo and holo forms provide details of the molecular mechanisms of activity and substrate specificity/inhibition of this enzyme.},
doi = {10.1107/S1399004715004228},
journal = {Acta Crystallographica. Section D: Biological Crystallography (Online)},
number = 5,
volume = 71,
place = {United States},
year = {Sat Apr 25 00:00:00 EDT 2015},
month = {Sat Apr 25 00:00:00 EDT 2015}
}
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