1v9m

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spinqualitylabelsall models 1v9m, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus

Overview

The V-type H(+)-ATPases are similar to the F-type ATP synthases in their, structure and functional mechanism. They hydrolyze ATP coupled with proton, translocation across a membrane, but in some archaea and eubacteria they, also synthesize ATP in the reverse reaction. The C subunit is one of the, components of the membrane-bound V(0) moiety of V-type ATPases. The C, subunit of V-type H(+)-ATPase from Thermus thermophilus was crystallized, in a monoclinic form and its crystal structure was determined at 1.85 A, resolution by the MAD method using selenomethionyl protein. The structure, has a cone (tapered cylinder) shape consisting of only two types of helix, (long and short) as secondary-structure elements. The molecule is divided, into three similar domains, each of which has essentially the same, topology. On the basis of the structural features and molecular-surface, charge distribution, it is suggested that the bottom side of the C subunit, is a possible binding site for the V(0) proteolipid L-subunit ring and, that the C subunit might function as a spacer unit between the proteolipid, L-subunit ring and the rotating V(1) central shaft.

About this Structure

1V9M is a Single protein structure of sequence from Thermus thermophilus with GOL as ligand. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.

Reference

Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution., Numoto N, Kita A, Miki K, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):810-5. Epub 2004, Apr 21. PMID:15103125

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