Heterogeneity in M. tuberculosis β-lactamase inhibition by Sulbactam

Malla, Tek Narsingh; Zielinski, Kara; Aldama, Luis; Bajt, Sasa; Feliz, Denisse; Hayes, Brendon; Hunter, Mark; Kupitz, Christopher; Lisova, Stella; Knoska, Juraj; Martin-Garcia, Jose Manuel; Mariani, Valerio; Pandey, Suraj; Poudyal, Ishwor; Sierra, Raymond G.; Tolstikova, Alexandra; Yefanov, Oleksandr; Yoon, Chung Hong; Ourmazd, Abbas; Fromme, Petra; Schwander, Peter; Barty, Anton; Chapman, Henry N.; Stojkovic, Emina A.; Batyuk, Alexander; Boutet, Sébastien; Phillips, Jr., George N.; Pollack, Lois; Schmidt, Marius

doi:10.1038/s41467-023-41246-1

Title: Heterogeneity in M. tuberculosis β-lactamase inhibition by Sulbactam

Journal Article · 07 September 2023 · Nature Communications

DOI: https://doi.org/10.1038/s41467-023-41246-1 · OSTI ID:1998844

^[1];

^[2]; Aldama, Luis ^[3]; Bajt, Sasa ^[4]; Feliz, Denisse ^[3]; Hayes, Brendon ^[5];

^[5]; Kupitz, Christopher ^[5]; Lisova, Stella ^[5]; Knoska, Juraj ^[6];

^[7]; Mariani, Valerio ^[5];

^[1]; Poudyal, Ishwor ^[1];

^[5]; Tolstikova, Alexandra ^[6]; Yefanov, Oleksandr ^[6];

^[5];

^[1];

^[8] more »

University of Wisconsin-Milwaukee, WI (United States)
Cornell University, Ithaca, NY (United States)
Northeastern Illinois University, Chicago, IL (United States)
Hamburg Centre for Ultrafast Imaging (Germany); Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany)
SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany)
Spanish National Research Council (CSIC), Madrid (Spain)
Arizona State University, Tempe, AZ (United States)
Hamburg Centre for Ultrafast Imaging (Germany); Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany); Universität Hamburg (Germany)
Rice University, Houston, TX (United States)

For decades, researchers have elucidated essential enzymatic functions on the atomic length scale by tracing atomic positions in real-time. Our work builds on possibilities unleashed by mix-and-inject serial crystallography (MISC) at X-ray free electron laser facilities. In this approach, enzymatic reactions are triggered by mixing substrate or ligand solutions with enzyme microcrystals. Here, we report in atomic detail (between 2.2 and 2.7 Å resolution) by room-temperature, time-resolved crystallography with millisecond time-resolution (with timepoints between 3 ms and 700 ms) how the Mycobacterium tuberculosis enzyme BlaC is inhibited by sulbactam (SUB). Our results reveal ligand binding heterogeneity, ligand gating, cooperativity, induced fit, and conformational selection all from the same set of MISC data, detailing how SUB approaches the catalytic clefts and binds to the enzyme noncovalently before reacting to a trans-enamine. This was made possible in part by the application of singular value decomposition to the MISC data using a program that remains functional even if unit cell parameters change up to 3 Å during the reaction.

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Research Organization:: University of Wisconsin-Milwaukee, WI (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Science Foundation (NSF); National Institutes of Health (NIH)

Grant/Contract Number:: SC0002164; NSF-1231306; STC-1231306; T34 GM105549; AC02-76SF00515

OSTI ID:: 1998844

Alternate ID(s):: OSTI ID: 1998574

Journal Information:: Nature Communications, Vol. 14, Issue 1; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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