Ontology highlight
ABSTRACT:
SUBMITTER: Rinaldi FC
PROVIDER: S-EPMC4531439 | biostudies-literature | 2015 Aug
REPOSITORIES: biostudies-literature
Rinaldi Fabio C FC Packer Michael M Collins Ruth R
BMC structural biology 20150812
<h4>Background</h4>Sec4p is a small monomeric Ras-related GTP-binding protein (23 kDa) that regulates polarized exocytosis in S. cerevisiae. In this study we examine the structural effects of a conserved serine residue in the P-loop corresponding to G12 in Ras.<h4>Results</h4>We show that the Sec4p residue serine 29 forms a hydrogen bond with the nucleotide. Mutations of this residue have a different impact than equivalent mutations in Ras and can form stable associations with the exchange facto ...[more]