Structure and dynamics of gamma-SNAP: insight into flexibility of proteins from the SNAP family.

TitleStructure and dynamics of gamma-SNAP: insight into flexibility of proteins from the SNAP family.
Publication TypeJournal Article
Year of Publication2008
AuthorsBitto E, Bingman CA, Kondrashov DA, McCoy JG, Bannen RM, Wesenberg GE, Phillips GN
Date Published2008 Jan 1
KeywordsAnimals, Cattle, Electrochemistry, Electrodes, Microscopy, Atomic Force, Protein Conformation, Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins

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.

Alternate JournalProteins
PubMed ID17634982
Grant List5T15LM007359 / LM / NLM NIH HHS / United States
P50 GM64598 / GM / NIGMS NIH HHS / United States
U54 GM074901 / GM / NIGMS NIH HHS / United States
Y1-CO-1020 / CO / NCI NIH HHS / United States
Y1-GM-1104 / GM / NIGMS NIH HHS / United States