2IFU

Crystal Structure of a Gamma-SNAP from Danio rerio

Summary for 2IFU

• Entry DOI: 10.2210/pdb2ifu/pdb
• Descriptor: gamma-snap, SULFATE ION (3 entities in total)
• Functional Keywords: gamma-snap, membrane fusion, snare complex disassembly, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Danio rerio (zebrafish)
• Total number of polymer chains: 4
• Total formula weight: 139302.75

Authors

Bitto, E.,Wesenberg, G.E.,Phillips Jr., G.N.,Mccoy, J.G.,Bingman, C.A.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2006-09-21, release date: 2006-10-10, Last modification date: 2024-11-13)

Primary citation

Bitto, E.,Bingman, C.A.,Kondrashov, D.A.,McCoy, J.G.,Bannen, R.M.,Wesenberg, G.E.,Phillips, G.N.
Structure and dynamics of gamma-SNAP: insight into flexibility of proteins from the SNAP family.
Proteins, 70:93-104, 2008

PubMed Abstract: 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.

PubMed: 17634982
DOI: 10.1002/prot.21468

Experimental method

X-RAY DIFFRACTION (2.6 Å)