Structural highlights
Publication Abstract from PubMed
Subunit "a" is associated with the membrane-bound (V(0)) complex of eukaryotic vacuolar H(+)-ATPase acidification machinery. It has also been shown recently to be involved in diverse membrane fusion/secretory functions independent of acidification. Here, we report the crystal structure of the N-terminal cytosolic domain from the Meiothermus ruber subunit "I" homolog of subunit a. The structure is composed of a curved long central alpha-helix bundle capped on both ends by two lobes with similar alpha/beta architecture. Based on the structure, a reasonable model of its eukaryotic subunit a counterpart was obtained. The crystal structure and model fit well into reconstruction densities from electron microscopy of prokaryotic and eukaryotic vacuolar H(+)-ATPases, respectively, clarifying their orientations and interactions and revealing features that could enable subunit a to play a role in membrane fusion/secretion.
Crystal Structure of the Cytoplasmic N-Terminal Domain of Subunit I, a Homolog of Subunit a, of V-ATPase.,Srinivasan S, Vyas NK, Baker ML, Quiocho FA J Mol Biol. 2011 Jul 22. PMID:21787787[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Srinivasan S, Vyas NK, Baker ML, Quiocho FA. Crystal Structure of the Cytoplasmic N-Terminal Domain of Subunit I, a Homolog of Subunit a, of V-ATPase. J Mol Biol. 2011 Jul 22. PMID:21787787 doi:10.1016/j.jmb.2011.07.014
