1ho8
|
CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE
OverviewOverview
In contrast to the F-type ATPases, which use a proton gradient to generate, ATP, the V-type enzymes use ATP to actively transport protons into, organelles and extracellular compartments. We describe here the structure, of the H-subunit (also called Vma13p) of the yeast enzyme. This is the, first structure of any component of a V-type ATPase. The H-subunit is not, required for assembly but plays an essential regulatory role. Despite the, lack of any apparent sequence homology the structure contains five motifs, similar to the so-called HEAT or armadillo repeats seen in the importins., A groove, which is occupied in the importins by the peptide that targets, proteins for import into the nucleus, is occupied here by the 10, amino-terminal residues of subunit H itself. The structural similarity, suggests how subunit H may interact with the ATPase itself or with other, proteins. A cleft between the amino- and carboxyl-terminal domains also, suggests another possible site of interaction with other factors.
About this StructureAbout this Structure
1HO8 is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 as ligand. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae., Sagermann M, Stevens TH, Matthews BW, Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7134-9. PMID:11416198
Page seeded by OCA on Tue Nov 20 16:42:29 2007