Results: 4

1.
Fig. 2.

Fig. 2. From: Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation.

Munc18a domain 3a β-hairpin loop. (A) A complex of Munc18a (blue, green, purple) and Syx1a (yellow) oriented to show the Munc18a β-hairpin loop and Syx1a SNARE domain. (B and C) Enlargements of the boxed regions showing the electron density (2Fo-Fc, contoured at 1 σ) for the complex of Munc18a and tag-free Syx1a (B) and Syx1aΔN (C). All electron density maps were generated with a 3.2-Å resolution cutoff.

Karen N. Colbert, et al. Proc Natl Acad Sci U S A. 2013 July 30;110(31):12637-12642.
2.
Fig. 3.

Fig. 3. From: Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation.

Comparison of Syx1a N-peptides. (A) Electron density (2Fo-Fc, contoured at 1 σ) of native Syx1a N-peptide (amino acids 2–9). (B) Overlay of native Syx1a N-peptide (yellow) with tagged Syx1a N-peptide [cyan, from 3C98 ()]; rmsd = 0.9 Å. (C) Overlay of native Syx1a N-peptide (yellow) with Syx4 [green, from 3PUJ ()]; rmsd = 1.2 Å. (D–F) Hydrogen bonds (dashed lines) formed between residues of Munc18a (white) and native Syx1a N-peptide (yellow; D), tagged Syx1a N-peptide (cyan; E), or Syx4 N-peptide (green; F). Side chains for Syx residues 6–9 were removed for clarity; Munc18a residues are underlined.

Karen N. Colbert, et al. Proc Natl Acad Sci U S A. 2013 July 30;110(31):12637-12642.
3.
Fig. 1.

Fig. 1. From: Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation.

Crystal structures of Munc18a bound to Syx1a with and without its native N terminus. (A) Different Syx1a constructs present in three separate Munc18a–Syx1a crystal structures. (B) Superposition of all three Munc18a–Syx1a structures. Munc18a [colored surface representation of domains 1 (blue), 2 (green), and 3a and 3b (purple)] from one structure only is shown for clarity. Reported in this work are structures of Munc18a bound to Syx1a in the presence (WT, yellow) and absence (ΔN, violet) of its native N terminus; the re-refined structure (3C98) of Munc18a bound to Syx1a bearing an N-terminal His6-tag (TAG, cyan) was published previously (). Syx1a N-peptide residues 10–26 were disordered (dashed line). Structural alignments yielded small rmsd values: WT and TAG (0.61 Å), WT and ΔN (0.61 Å), and TAG and ΔN (0.60 Å).

Karen N. Colbert, et al. Proc Natl Acad Sci U S A. 2013 July 30;110(31):12637-12642.
4.
Fig. 4.

Fig. 4. From: Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation.

Scattering curves and SAXS-derived parameters for Munc18a–Syx1a complexes. (A) SAXS data for Munc18a bound to Syx1a in the presence (WT, yellow) and absence (ΔN, violet) of its native N terminus, and for Munc18a bound to Syx1a L165A/E166A (LE, cyan), offset on the y- axis for clarity. Solid lines represent the scattering curves calculated from the Munc18a–Syx1a structure [fit to the experimental curves for WT (χ2 = 1.6) and LE (χ2 = 1.6)] and from the Munc18a–Syx1aΔN structure [fit to the ΔN experimental curve (χ2 = 1.5)]. Experimental curves were merged from scattering curves at two concentrations, 1 mg/mL and 4 mg/mL. (Inset) Guinier regions for each of the Munc18a–Syx1a complexes. (B) The pair distance distribution function, P(r), calculated using the indirect Fourier transform method in GNOM () from the scattering curves in A for each of the Munc18a–Syx1a complexes. P(r) plots are color-coded as in A.

Karen N. Colbert, et al. Proc Natl Acad Sci U S A. 2013 July 30;110(31):12637-12642.

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