1HO8

CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE

Summary for 1HO8

• Entry DOI: 10.2210/pdb1ho8/pdb
• Descriptor: VACUOLAR ATP SYNTHASE SUBUNIT H, SULFATE ION (3 entities in total)
• Functional Keywords: heat repeat, hydrolase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 54722.80

Authors

Sagermann, M.,Stevens, T.H.,Matthews, B.W. (deposition date: 2000-12-10, release date: 2001-06-20, Last modification date: 2024-04-03)

Primary citation

Sagermann, M.,Stevens, T.H.,Matthews, B.W.
Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae.
Proc.Natl.Acad.Sci.USA, 98:7134-7139, 2001

PubMed Abstract: 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.

PubMed: 11416198
DOI: 10.1073/pnas.131192798

Experimental method

X-RAY DIFFRACTION (2.95 Å)