2ifu
Crystal Structure of a Gamma-SNAP from Danio rerio
OverviewOverview
Soluble N-ethylmaleimide-sensitive factor attachment protein gamma (gamma-SNAP) is a member of an eukaryotic protein family involved in intracellular membrane trafficking. The X-ray structure of Brachydanio rerio gamma-SNAP was determined to 2.6 A and revealed an all-helical protein comprised of an extended twisted-sheet of helical hairpins with a helical-bundle domain on its carboxy-terminal end. Structural and conformational differences between multiple observed gamma-SNAP molecules and Sec17, a SNAP family protein from yeast, are analyzed. Conformational variation in gamma-SNAP molecules is matched with great precision by the two lowest frequency normal modes of the structure. Comparison of the lowest-frequency modes from gamma-SNAP and Sec17 indicated that the structures share preferred directions of flexibility, corresponding to bending and twisting of the twisted sheet motif. We discuss possible consequences related to the flexibility of the SNAP proteins for the mechanism of the 20S complex disassembly during the SNAP receptors recycling.
About this StructureAbout this Structure
2IFU is a Single protein structure of sequence from Danio rerio. Full crystallographic information is available from OCA.
ReferenceReference
Structure and dynamics of gamma-SNAP: insight into flexibility of proteins from the SNAP family., Bitto E, Bingman CA, Kondrashov DA, McCoy JG, Bannen RM, Wesenberg GE, Phillips GN Jr, Proteins. 2008 Jan 1;70(1):93-104. PMID:17634982 Page seeded by OCA on Sun May 4 07:27:15 2008