Literature DB >> 11898864

Structure of the vacuolar adenosine triphosphatases.

S Wilkens1.   

Abstract

Vacuolar adenosine triphosphatases (V-ATPases) represent an important class of proton pumps found in endomembrane systems of eucaryotic cells, where they are involved in pH regulation. Progress has been made in the structure determination of this large, membrane-bound multisubunit enzyme complex. Electron microscopy of the V-ATPase has revealed a ball-and-stalk-like structure similar to F1F0-type ATP synthase, to which the V-ATPase is evolutionary related. Aside from the overall structural similarity of the V-ATPase and F-ATP synthase, a number of distinct structural differences exist between the two related enzymes, giving clues to their different function and regulation in the organism.

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Year:  2001        PMID: 11898864     DOI: 10.1385/CBB:34:2:191

Source DB:  PubMed          Journal:  Cell Biochem Biophys        ISSN: 1085-9195            Impact factor:   2.194


  1 in total

1.  Crystal structure of subunits D and F in complex gives insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae.

Authors:  Asha Manikkoth Balakrishna; Sandip Basak; Malathy Sony Subramanian Manimekalai; Gerhard Grüber
Journal:  J Biol Chem       Date:  2014-12-12       Impact factor: 5.157

  1 in total

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