The crystal structure of TV0924.

<p>A cartoon representation of the model is shown, with helices in green, β-strands in purple, and regions without regular secondary structure in light blue. The amino- and carboxyl-termini are labeled “N” and “C”, respectively. The region encompassing putative active-site residues is circled...

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Bibliographic Details
Main Author:	Ranjit K. Deka (15626723) (author)
Other Authors:	Shih-Chia Tso (3704401) (author), Wei Z. Liu (3044511) (author), Chad A. Brautigam (242609) (author)
Published:	2025
Subjects:	Biophysics Biochemistry Microbiology Genetics Molecular Biology Evolutionary Biology Infectious Diseases Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified related treponemal species microaerophilic host environments cycle enzymes suggested alternative sources could evidence strongly supported treponema vincentii </ biochemical evidence supports second crystal structure named tp0476 ), div >< p acid sequence identity known acetate kinases alternative energy source treponema pallidum </ 3 å resolution biochemical evidence crystal structure energy source acetate kinases pallidum </ 36 å acetogenic energy acetate kinase sole carbon similar fold recent bioinformatic provided insight parasitic spirochete ostensibly catalyzes oral pathogen key component human disease homologous enzyme final enzyme enzyme ’ enzyme exists enzymatic activity
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The crystal structure of TV0924.

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