1ez3
From Proteopedia
(New page: 200px<br /><applet load="1ez3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ez3, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1ez3.jpg|left|200px]]<br /><applet load="1ez3" size=" | + | [[Image:1ez3.jpg|left|200px]]<br /><applet load="1ez3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ez3, resolution 1.90Å" /> | caption="1ez3, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE OF THE NEURONAL T-SNARE SYNTAXIN-1A'''<br /> | '''CRYSTAL STRUCTURE OF THE NEURONAL T-SNARE SYNTAXIN-1A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Intracellular trafficking depends on the docking and fusion of transport | + | Intracellular trafficking depends on the docking and fusion of transport vesicles with cellular membranes. Central to docking and fusion is the pairing of SNARE proteins (soluble NSF attachment protein receptors) associated with the vesicle and target membranes (v- and t-SNAREs, respectively). Here, the X-ray structure of an N-terminal conserved domain of the neuronal t-SNARE syntaxin-1A was determined to a resolution of 1.9 A using multiwavelength anomalous diffraction. This X-ray structure, which is in general agreement with an NMR structure of a similar fragment, provides new insight into the interaction surface between the N-terminal domain and the remainder of the protein. In vitro characterization of the intact cytoplasmic domain of syntaxin revealed that it forms dimers, and probably tetramers, at low micromolar concentrations, with concomitant structural changes that can be detected by limited proteolysis. These observations suggest that the promiscuity characteristic of pairing between v-SNAREs and t-SNAREs extends to the formation of homo-oligomeric t-SNARE complexes as well. They also suggest a potential role for the neuronal Sec1 protein (nSec1) in preventing the formation of syntaxin multimers. |
==About this Structure== | ==About this Structure== | ||
| - | 1EZ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1EZ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1EZ3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fairman, R.]] | [[Category: Fairman, R.]] | ||
| - | [[Category: Hughson, F | + | [[Category: Hughson, F M.]] |
| - | [[Category: Lerman, J | + | [[Category: Lerman, J C.]] |
[[Category: Robblee, J.]] | [[Category: Robblee, J.]] | ||
[[Category: three helix bundle]] | [[Category: three helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:06 2008'' |
Revision as of 10:33, 21 February 2008
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CRYSTAL STRUCTURE OF THE NEURONAL T-SNARE SYNTAXIN-1A
Overview
Intracellular trafficking depends on the docking and fusion of transport vesicles with cellular membranes. Central to docking and fusion is the pairing of SNARE proteins (soluble NSF attachment protein receptors) associated with the vesicle and target membranes (v- and t-SNAREs, respectively). Here, the X-ray structure of an N-terminal conserved domain of the neuronal t-SNARE syntaxin-1A was determined to a resolution of 1.9 A using multiwavelength anomalous diffraction. This X-ray structure, which is in general agreement with an NMR structure of a similar fragment, provides new insight into the interaction surface between the N-terminal domain and the remainder of the protein. In vitro characterization of the intact cytoplasmic domain of syntaxin revealed that it forms dimers, and probably tetramers, at low micromolar concentrations, with concomitant structural changes that can be detected by limited proteolysis. These observations suggest that the promiscuity characteristic of pairing between v-SNAREs and t-SNAREs extends to the formation of homo-oligomeric t-SNARE complexes as well. They also suggest a potential role for the neuronal Sec1 protein (nSec1) in preventing the formation of syntaxin multimers.
About this Structure
1EZ3 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural analysis of the neuronal SNARE protein syntaxin-1A., Lerman JC, Robblee J, Fairman R, Hughson FM, Biochemistry. 2000 Jul 25;39(29):8470-9. PMID:10913252
Page seeded by OCA on Thu Feb 21 12:33:06 2008
