3a5d | pdb_00003a5d

Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase

spinqualitylabelsall models 3a5d, resolution 4.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3a5d is a 16 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3a5c Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed V-type ATPases (V-ATPases) are categorized as rotary ATP synthase/ATPase complexes. The V-ATPases are distinct from F-ATPases in terms of their rotation scheme, architecture and subunit composition. However, there is no detailed structural information on V-ATPases despite the abundant biochemical and biophysical research. Here, we report a crystallographic study of V1-ATPase, from Thermus thermophilus, which is a soluble component consisting of A, B, D and F subunits. The structure at 4.5 A resolution reveals inter-subunit interactions and nucleotide binding. In particular, the structure of the central stalk composed of D and F subunits was shown to be characteristic of V1-ATPases. Small conformational changes of respective subunits and significant rearrangement of the quaternary structure observed in the three AB pairs were related to the interaction with the straight central stalk. The rotation mechanism is discussed based on a structural comparison between V1-ATPases and F1-ATPases. Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase.,Numoto N, Hasegawa Y, Takeda K, Miki K EMBO Rep. 2009 Nov;10(11):1228-34. Epub 2009 Sep 25. PMID:19779483 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase V-ATPase

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