Overview
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Key numbers
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- apart (24, 26). In contrast, the closed state is reported for the pre- LfArsA has 69% sequence identity to EcArsA, retaining all the
- 29), supporting that crystallization has likely restricted the range ArsA·MgADP state (Fig. 1A). The final Coulomb potential map
- metalloid affinity of this site (29, 30). As the crystal structures are good resolvability of the cryo-EM map (36). About 95% of the
- ture to the X-ray crystal structures of EcArsA reveals the structures resolvability of the cryo-EM map. About 97% of the protein was
- ArsA·MgADP, gray; ArsA C114A/C173A/C422A·MgADP, yellow). Bars represent mean As/ArsA molar ratio for n = 3 individually prepared samples with error bars
- and 5 mM ATP at 37ºC (wild-type, black; C173A, teal; C114A/C173A/C422A, yellow). Data points represent mean of n = 3, and error bars represent SD. The data
- SI Appendix, Table S2). Similar AsIII coordination has been and closed states. Upon AsIII binding to the metalloid-binding site
- on XAS analysis (15, 39, 40). We quantified the amount of AsIII rearrangement such that the N-terminal end of each helix, bearing
- ICP-MS analysis of this variant shows over 50% decrease in His453 (H7C) form a π–π stacking interaction (SI Appendix,
- domains such that Cys114 on H6N and Cys422 on H6C shift ~9 (Fig. 4F). Complete helical rearrangement of H7N arises by virtue
- of Cys114 and Cys442 accompanies this conformational rearrange- a considerable rearrangement between the open and closed states
- in the N-domain (Fig. 4 C and G). While the carboxylate group of micromolar range (14). On the other hand, there is no biochemical
- Fig. 4. Intradomain conformational changes between ADP-open and ATP-closed states. (A and B) Cartoon representations of overall structural rearrangements
- P-loops (residues 16 to 23 for N-domain and 334 to 341 for C-domain). (C and D) Conformational changes in Switch I motif between open (50% opacity) and
- closed (100% opacity) states at both N-and C-nucleotide binding sites, respectively. Shift in the carboxylate group of catalytic Asp from open to closed states is
- indicated in Å. (E) Conformational changes in Switch II and H7N of the N-domain between open (50% opacity) and closed (100% opacity) states, shown in two
- between open (50% opacity) and closed (100% opacity) states. In both panels E and F, helix 6 has been omitted for visual clarity. (G) Comparison of Switch I and
Methods (brief)
- loid (27, 28). X-ray crystal structures of Escherichia coli ArsA particle analysis. From a dataset of 4,732 movies collected on a
- the presence of millimolar concentrations AsIII in the samples, there Within both nucleotide-binding sites, ATP is stabilized by elec-
- To confirm the AsIII coordination environment, we performed carbon scattering was also observed in the sample, likely from
- with best-fit simulations (green) for each complex. Right column, corresponding Fourier transforms. A replicate of each XAS sample was individually prepared
- and analyzed (SI Appendix, Fig. S13). (C) ICP-MS analysis for AsIII quantification in nucleotide-bound LfArsA samples (ArsA·MgATP, black; ArsA C173A·MgATP, teal;
- ArsA·MgADP, gray; ArsA C114A/C173A/C422A·MgADP, yellow). Bars represent mean As/ArsA molar ratio for n = 3 individually prepared samples with error bars
- state and coordination environment of the ArsA sample are Switch II, acting as a link between the nucleotide-binding site
- consistent with that of a control sample consisting of AsIII and and the metalloid-binding site, modulates a series of dramatic
- sample preparation using inductively coupled plasma mass spec- from the nucleotide-binding sites (Fig. 4 A and B). Reorientation
- trometry (ICP-MS). In the presence of MgATP, ArsA binds AsIII of helix 6 results in the restructuring of the downstream Switch
- cryo-EM, XAS, and ICP-MS analysis support the binding of a (Asp143 and Asp447) of the respective domains remain anchored
- ICP-MS analysis of this variant shows over 50% decrease in His453 (H7C) form a π–π stacking interaction (SI Appendix,
- Based on our ICP-MS analysis, ArsA·MgADP binds AsIII far ADP-open state, H7N is composed of residues Gly148-Leu154.
- N- and C-domains in the closed state (Fig. 4G and SI Appendix, formed using Phenix (47) and Coot (48). Detailed procedures for cryo-EM sample
- ATPase domain and that the ATPase activity is only required to and ICP-MS plots can be accessed in the same GitHub repository as well.
- the ability of ArsB to remove AsIII (45), implying that the inactive Interactions at Caltech (S.M.). Cryo-EM data were collected at the Caltech Cryo-EM
- change in ArsB to facilitate metalloid transport, or by increasing lection and processing. XAS data were collected on beamline 7-3 at the Stanford
- of ArsA enables the formation of a transient high-affinity metalloid well as Jens T. Kaiser for his assistance with preparing and shipping XAS samples.
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Update history
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