1urq: Difference between revisions

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[[Image:1urq.gif|left|200px]]<br /><applet load="1urq" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1urq.gif|left|200px]]<br /><applet load="1urq" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1urq, resolution 2.000Å" />

'''CRYSTAL STRUCTURE OF NEURONAL Q-SNARES IN COMPLEX WITH R-SNARE MOTIF OF TOMOSYN'''<br />

==Overview==

Upon Ca2+ influx synaptic vesicles fuse with the plasma membrane and, release their neurotransmitter cargo into the synaptic cleft. Key players, during this process are the Q-SNAREs syntaxin 1a and SNAP-25 and the, R-SNARE synaptobrevin 2. It is thought that these membrane proteins, gradually assemble into a tight trans-SNARE complex between vesicular and, plasma membrane, ultimately leading to membrane fusion. Tomosyn is a, soluble protein of 130 kDa that contains a COOH-terminal R-SNARE motif but, lacks a transmembrane anchor. Its R-SNARE motif forms a stable core SNARE, complex with syntaxin 1a and SNAP-25. Here we present the crystal, structure of this core tomosyn SNARE complex at 2.0-A resolution. It, consists of a four-helical bundle very similar to that of the SNARE, complex containing synaptobrevin. Most differences are found on the, surface, where they prevented tight binding of complexin. Both complexes, form with similar rates as assessed by CD spectroscopy. In addition, synaptobrevin cannot displace the tomosyn helix from the tight complex and, vice versa, indicating that both SNARE complexes represent end products., Moreover, data bank searches revealed that the R-SNARE motif of tomosyn is, highly conserved throughout all eukaryotic kingdoms. This suggests that, the formation of a tight SNARE complex is important for the function of, tomosyn.

Upon Ca2+ influx synaptic vesicles fuse with the plasma membrane and release their neurotransmitter cargo into the synaptic cleft. Key players during this process are the Q-SNAREs syntaxin 1a and SNAP-25 and the R-SNARE synaptobrevin 2. It is thought that these membrane proteins gradually assemble into a tight trans-SNARE complex between vesicular and plasma membrane, ultimately leading to membrane fusion. Tomosyn is a soluble protein of 130 kDa that contains a COOH-terminal R-SNARE motif but lacks a transmembrane anchor. Its R-SNARE motif forms a stable core SNARE complex with syntaxin 1a and SNAP-25. Here we present the crystal structure of this core tomosyn SNARE complex at 2.0-A resolution. It consists of a four-helical bundle very similar to that of the SNARE complex containing synaptobrevin. Most differences are found on the surface, where they prevented tight binding of complexin. Both complexes form with similar rates as assessed by CD spectroscopy. In addition, synaptobrevin cannot displace the tomosyn helix from the tight complex and vice versa, indicating that both SNARE complexes represent end products. Moreover, data bank searches revealed that the R-SNARE motif of tomosyn is highly conserved throughout all eukaryotic kingdoms. This suggests that the formation of a tight SNARE complex is important for the function of tomosyn.

==About this Structure==

1URQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1URQ OCA].

1URQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URQ OCA].

==Reference==

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[[Category: tomosyn-snare complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 04:18:~~02 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:37 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1urq.gif|left|200px]]<br /><applet load="1urq" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1urq.gif|left|200px]]<br /><applet load="1urq" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1urq, resolution 2.000&Aring;" />
 '''CRYSTAL STRUCTURE OF NEURONAL Q-SNARES IN COMPLEX WITH R-SNARE MOTIF OF TOMOSYN'''<br />
 ==Overview==
-Upon Ca2+ influx synaptic vesicles fuse with the plasma membrane and, release their neurotransmitter cargo into the synaptic cleft. Key players, during this process are the Q-SNAREs syntaxin 1a and SNAP-25 and the, R-SNARE synaptobrevin 2. It is thought that these membrane proteins, gradually assemble into a tight trans-SNARE complex between vesicular and, plasma membrane, ultimately leading to membrane fusion. Tomosyn is a, soluble protein of 130 kDa that contains a COOH-terminal R-SNARE motif but, lacks a transmembrane anchor. Its R-SNARE motif forms a stable core SNARE, complex with syntaxin 1a and SNAP-25. Here we present the crystal, structure of this core tomosyn SNARE complex at 2.0-A resolution. It, consists of a four-helical bundle very similar to that of the SNARE, complex containing synaptobrevin. Most differences are found on the, surface, where they prevented tight binding of complexin. Both complexes, form with similar rates as assessed by CD spectroscopy. In addition, synaptobrevin cannot displace the tomosyn helix from the tight complex and, vice versa, indicating that both SNARE complexes represent end products., Moreover, data bank searches revealed that the R-SNARE motif of tomosyn is, highly conserved throughout all eukaryotic kingdoms. This suggests that, the formation of a tight SNARE complex is important for the function of, tomosyn.
+Upon Ca2+ influx synaptic vesicles fuse with the plasma membrane and release their neurotransmitter cargo into the synaptic cleft. Key players during this process are the Q-SNAREs syntaxin 1a and SNAP-25 and the R-SNARE synaptobrevin 2. It is thought that these membrane proteins gradually assemble into a tight trans-SNARE complex between vesicular and plasma membrane, ultimately leading to membrane fusion. Tomosyn is a soluble protein of 130 kDa that contains a COOH-terminal R-SNARE motif but lacks a transmembrane anchor. Its R-SNARE motif forms a stable core SNARE complex with syntaxin 1a and SNAP-25. Here we present the crystal structure of this core tomosyn SNARE complex at 2.0-A resolution. It consists of a four-helical bundle very similar to that of the SNARE complex containing synaptobrevin. Most differences are found on the surface, where they prevented tight binding of complexin. Both complexes form with similar rates as assessed by CD spectroscopy. In addition, synaptobrevin cannot displace the tomosyn helix from the tight complex and vice versa, indicating that both SNARE complexes represent end products. Moreover, data bank searches revealed that the R-SNARE motif of tomosyn is highly conserved throughout all eukaryotic kingdoms. This suggests that the formation of a tight SNARE complex is important for the function of tomosyn.
 ==About this Structure==
-URQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1URQ OCA].
+URQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URQ OCA].
 ==Reference==
@@ Line 22: / Line 22: @@
 [[Category: tomosyn-snare complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:18:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:37 2008''