Solution structure and dynamics of the mitochondrial‐targeted GTPase ‐activating protein (GAP) VopE by an integrated NMR / SAXS approach

Smith, Kyle P.; Lee, Woonghee; Tonelli, Marco; Lee, Yeongjoon; Light, Samuel H.; Cornilescu, Gabriel; Chakravarthy, Srinivas

doi:10.1002/pro.4282

Title: Solution structure and dynamics of the mitochondrial‐targeted GTPase ‐activating protein (GAP) VopE by an integrated NMR / SAXS approach

Journal Article · 27 April 2022 · Protein Science

DOI: https://doi.org/10.1002/pro.4282 · OSTI ID:1870042

^[1];

^[2]; Tonelli, Marco ^[3]; Lee, Yeongjoon ^[2]; Light, Samuel H. ^[4]; Cornilescu, Gabriel ^[5]; Chakravarthy, Srinivas ^[6]

Department of Cell &, Developmental Biology Northwestern University Chicago Illinois USA, Xilio Therapeutics Waltham Massachusetts USA
Department of Chemistry University of Colorado‐Denver Denver Colorado USA
National Magnetic Resonance Facility at Madison, Department of Biochemistry University of Wisconsin‐Madison Madison Wisconsin USA
Department of Microbiology University of Chicago Chicago Illinois USA
Advanced Technology Research Facility, Frederick National Laboratory for Cancer Research Leidos Biomedical Research, Inc., National Cancer Institute, National Institutes of Health Frederick Maryland USA
Biophysics Collaborative Access Team Argonne National Laboratory Argonne Illinois USA

Abstract The bacterial pathogen Vibrio cholerae use a type III secretion system to inject effector proteins into a host cell. Recently, a putative Toxic GTPase Activating Protein (ToxGAP) called Vibrio outer protein E (VopE) was identified as a T3SS substrate and virulence factor that affected host mitochondrial dynamics and immune response. However, biophysical and structural characterization has been absent. Here, we describe solution NMR structure of the putative GTPase‐activating protein (GAP) domain (73–204) of VopE. Using size exclusion chromatography coupled with small‐angle x‐ray scattering and residual dipolar coupling data, we restrained the MD process to efficiently determine the overall fold and improve the quality of the output calculated structures. Comparing the structure of VopE with other ToxGAP's revealed a similar overall fold with several features unique to VopE. Specifically, the “Bulge 1,” α1 helix, and noteworthy “backside linker” elements on the N‐terminus are dissimilar to the other ToxGAP's. By using NMR relaxation dispersion experiments, we demonstrate that these regions undergo motions on a > 6 s ⁻¹ timescale. Based on the disposition of these mobile regions relative to the putative catalytic arginine residue, we hypothesize that the protein may undergo structural changes to bind cognate GTPases.

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Sponsoring Organization:: USDOE

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1870042

Journal Information:: Protein Science, Journal Name: Protein Science Journal Issue: 5 Vol. 31; ISSN 0961-8368

Publisher:: Wiley Blackwell (John Wiley & Sons)Copyright Statement

Country of Publication:: United Kingdom

Language:: English

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