Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain
Steven J. Freedman, Hyun Kyu Song, Yingwu Xu, Zhen Yu J. Sun, Michael J. Eck
SNARE proteins mediate intracellular membrane fusion by forming a coiled-coil complex to merge opposing membranes. A "fusion-active" neuronal SNARE complex is a parallel four-helix bundle containing two coiled-coil domains from SNAP-25 and one coiled-coil domain each from syntaxin-la and VAMP-2. "Prefusion" assembly intermediate complexes can also form from these SNAREs. We studied the N-terminal coiled-coil domain of SNAP-23 (SNAP-23N), a non-neuronal homologue of SNAP-25, and its interaction with other coiled-coil domains. SNAP-23N can assemble spontaneously with the coiled-coil domains from SNAP-23C, syntaxin-4, and VAMP-3 to form a heterotetrameric complex. Unexpectedly, pure SNAP-23N crystallizes as a coiled-coil homotetrameric complex. The four helices have a parallel orientation and are symmetrical about the long axis. The complex is stabilized through the interaction of conserved hydrophobic residues comprising the a and d positions of the coiled-coil heptad repeats. In addition, a central, highly conserved glutamine residue (Gln-48) is buried within the interface by hydrogen bonding between glutamine side chains derived from adjacent subunits and to solvent molecules. A comparison of the SNAP-23N structure to other SNARE complex structures reveals how a simple coiled-coil motif can form diverse SNARE complexes.
https://doi.org/10.1074/jbc.M210483200
Published - 2003 Apr 11
10.1074/jbc.M210483200
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Glutamine Residue Chemical Compounds 100%
SNARE Proteins Medicine & Life Sciences 90%
Glutamine Chemical Compounds 75%
Qa-SNARE Proteins Medicine & Life Sciences 39%
Hydrogen Chemical Compounds 34%
Purity Chemical Compounds 34%
Solvent Chemical Compounds 31%
Freedman, S. J., Song, H. K., Xu, Y., Sun, Z. Y. J., & Eck, M. J. (2003). Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain. Journal of Biological Chemistry, 278(15), 13462-13467. https://doi.org/10.1074/jbc.M210483200
Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain. / Freedman, Steven J.; Song, Hyun Kyu; Xu, Yingwu; Sun, Zhen Yu J.; Eck, Michael J.
In: Journal of Biological Chemistry, Vol. 278, No. 15, 11.04.2003, p. 13462-13467.
Freedman, SJ, Song, HK, Xu, Y, Sun, ZYJ & Eck, MJ 2003, 'Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain', Journal of Biological Chemistry, vol. 278, no. 15, pp. 13462-13467. https://doi.org/10.1074/jbc.M210483200
Freedman SJ, Song HK, Xu Y, Sun ZYJ, Eck MJ. Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain. Journal of Biological Chemistry. 2003 Apr 11;278(15):13462-13467. https://doi.org/10.1074/jbc.M210483200
Freedman, Steven J. ; Song, Hyun Kyu ; Xu, Yingwu ; Sun, Zhen Yu J. ; Eck, Michael J. / Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain. In: Journal of Biological Chemistry. 2003 ; Vol. 278, No. 15. pp. 13462-13467.
@article{8baaf04688e5462bb9aee1741bca2df7,
title = "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain",
abstract = "SNARE proteins mediate intracellular membrane fusion by forming a coiled-coil complex to merge opposing membranes. A {"}fusion-active{"} neuronal SNARE complex is a parallel four-helix bundle containing two coiled-coil domains from SNAP-25 and one coiled-coil domain each from syntaxin-la and VAMP-2. {"}Prefusion{"} assembly intermediate complexes can also form from these SNAREs. We studied the N-terminal coiled-coil domain of SNAP-23 (SNAP-23N), a non-neuronal homologue of SNAP-25, and its interaction with other coiled-coil domains. SNAP-23N can assemble spontaneously with the coiled-coil domains from SNAP-23C, syntaxin-4, and VAMP-3 to form a heterotetrameric complex. Unexpectedly, pure SNAP-23N crystallizes as a coiled-coil homotetrameric complex. The four helices have a parallel orientation and are symmetrical about the long axis. The complex is stabilized through the interaction of conserved hydrophobic residues comprising the a and d positions of the coiled-coil heptad repeats. In addition, a central, highly conserved glutamine residue (Gln-48) is buried within the interface by hydrogen bonding between glutamine side chains derived from adjacent subunits and to solvent molecules. A comparison of the SNAP-23N structure to other SNARE complex structures reveals how a simple coiled-coil motif can form diverse SNARE complexes.",
author = "Freedman, {Steven J.} and Song, {Hyun Kyu} and Yingwu Xu and Sun, {Zhen Yu J.} and Eck, {Michael J.}",
doi = "10.1074/jbc.M210483200",
T1 - Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain
AU - Freedman, Steven J.
AU - Song, Hyun Kyu
AU - Xu, Yingwu
AU - Sun, Zhen Yu J.
AU - Eck, Michael J.
N2 - SNARE proteins mediate intracellular membrane fusion by forming a coiled-coil complex to merge opposing membranes. A "fusion-active" neuronal SNARE complex is a parallel four-helix bundle containing two coiled-coil domains from SNAP-25 and one coiled-coil domain each from syntaxin-la and VAMP-2. "Prefusion" assembly intermediate complexes can also form from these SNAREs. We studied the N-terminal coiled-coil domain of SNAP-23 (SNAP-23N), a non-neuronal homologue of SNAP-25, and its interaction with other coiled-coil domains. SNAP-23N can assemble spontaneously with the coiled-coil domains from SNAP-23C, syntaxin-4, and VAMP-3 to form a heterotetrameric complex. Unexpectedly, pure SNAP-23N crystallizes as a coiled-coil homotetrameric complex. The four helices have a parallel orientation and are symmetrical about the long axis. The complex is stabilized through the interaction of conserved hydrophobic residues comprising the a and d positions of the coiled-coil heptad repeats. In addition, a central, highly conserved glutamine residue (Gln-48) is buried within the interface by hydrogen bonding between glutamine side chains derived from adjacent subunits and to solvent molecules. A comparison of the SNAP-23N structure to other SNARE complex structures reveals how a simple coiled-coil motif can form diverse SNARE complexes.
AB - SNARE proteins mediate intracellular membrane fusion by forming a coiled-coil complex to merge opposing membranes. A "fusion-active" neuronal SNARE complex is a parallel four-helix bundle containing two coiled-coil domains from SNAP-25 and one coiled-coil domain each from syntaxin-la and VAMP-2. "Prefusion" assembly intermediate complexes can also form from these SNAREs. We studied the N-terminal coiled-coil domain of SNAP-23 (SNAP-23N), a non-neuronal homologue of SNAP-25, and its interaction with other coiled-coil domains. SNAP-23N can assemble spontaneously with the coiled-coil domains from SNAP-23C, syntaxin-4, and VAMP-3 to form a heterotetrameric complex. Unexpectedly, pure SNAP-23N crystallizes as a coiled-coil homotetrameric complex. The four helices have a parallel orientation and are symmetrical about the long axis. The complex is stabilized through the interaction of conserved hydrophobic residues comprising the a and d positions of the coiled-coil heptad repeats. In addition, a central, highly conserved glutamine residue (Gln-48) is buried within the interface by hydrogen bonding between glutamine side chains derived from adjacent subunits and to solvent molecules. A comparison of the SNAP-23N structure to other SNARE complex structures reveals how a simple coiled-coil motif can form diverse SNARE complexes.
U2 - 10.1074/jbc.M210483200
DO - 10.1074/jbc.M210483200