1S94

Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei

Summary for 1S94

• Entry DOI: 10.2210/pdb1s94/pdb
• Related: 1BR0 1DN1 1EPU 1EZ3 1L4A
• Descriptor: s-syntaxin (1 entity in total)
• Functional Keywords: three helix bundle, structural plasticity, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Loligo pealei
• Total number of polymer chains: 2
• Total formula weight: 41430.44

Authors

Bracher, A.,Weissenhorn, W. (deposition date: 2004-02-03, release date: 2004-05-11, Last modification date: 2024-10-30)

Primary citation

Bracher, A.,Weissenhorn, W.
Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminus
BMC STRUCT.BIOL., 4:6-6, 2004

PubMed Abstract: 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.

PubMed: 15113421
DOI: 10.1186/1472-6807-4-6

Experimental method

X-RAY DIFFRACTION (3.34 Å)