1s94
From Proteopedia
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| - | [[Image:1s94.gif|left|200px]] | + | [[Image:1s94.gif|left|200px]] |
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| - | '''Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei''' | + | {{Structure |
| + | |PDB= 1s94 |SIZE=350|CAPTION= <scene name='initialview01'>1s94</scene>, resolution 3.34Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S94 is a [ | + | 1S94 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Loligo_plei Loligo plei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S94 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminus., Bracher A, Weissenhorn W, BMC Struct Biol. 2004 Mar 15;4:6. PMID:[http:// | + | Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminus., Bracher A, Weissenhorn W, BMC Struct Biol. 2004 Mar 15;4:6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15113421 15113421] |
[[Category: Loligo plei]] | [[Category: Loligo plei]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: three helix bundle]] | [[Category: three helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:01:54 2008'' |
Revision as of 12:01, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei
Overview
BACKGROUND: Intracellular membrane fusion processes are mediated by the spatial and temporal control of SNARE complex assembly that results in the formation of a four-helical bundle, composed of one vesicle SNARE and three target membrane SNARE polypeptide chains. Syntaxins are essential t-SNAREs and are characterized by an N-terminal Habc domain, a flexible linker region, a coiled-coil or SNARE motif and a membrane anchor. The N-terminal Habc domain fulfills important regulatory functions while the coiled-coil motif, present in all SNAREs, is sufficient for SNARE complex formation, which is thought to drive membrane fusion. RESULTS: Here we report the crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei, s-syntaxin. Squid Habc crystallizes as a dimer and the monomer structure consists of a three-helical bundle. One molecule is strikingly similar to mammalian syntaxin 1A while the second one shows a structural deviation from the common fold in that the C-terminal part of helix C unwinds and adopts an extended conformation. CONCLUSION: Conservation of surface residues indicates that the cytosolic part of s-syntaxin can adopt an auto-inhibitory closed conformation that may bind squid neuronal Sec1, s-Sec1, in the same manner as observed in structure of the rat nSec1/syntaxin 1A complex. Furthermore, despite the overall structural similarity, the observed changes at the C-terminus of one molecule indicate structural plasticity in neuronal syntaxin. Implications of the structural conservation and the changes are discussed with respect to potential Habc domain binding partners such as Munc13, which facilitates the transition from the closed to the open conformation.
About this Structure
1S94 is a Single protein structure of sequence from Loligo plei. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminus., Bracher A, Weissenhorn W, BMC Struct Biol. 2004 Mar 15;4:6. PMID:15113421
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