1V9M

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

Summary for 1V9M

• Entry DOI: 10.2210/pdb1v9m/pdb
• Descriptor: V-type ATP synthase subunit C, GLYCEROL (3 entities in total)
• Functional Keywords: vov1-atpase, v-type atpase, the c subunit, thermus thermophilus, riken structural genomics/proteomics initiative, rsgi, structural genomics, hydrolase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 36152.76

Authors

Numoto, N.,Kita, A.,Miki, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-01-26, release date: 2004-05-04, Last modification date: 2024-10-30)

Primary citation

Numoto, N.,Kita, A.,Miki, K.
Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution.
Acta Crystallogr.,Sect.D, 60:810-815, 2004

PubMed Abstract: 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.

PubMed: 15103125
DOI: 10.1107/S0907444904003257

Experimental method

X-RAY DIFFRACTION (1.85 Å)