ATPases structure

Recent review articles on Na,K-ATPase structure and function... 

In comparing NaVK+-ATPase structures to those of other P-type ATPases, we find that available structures for the NaVK+-ATPase system are not as robust and informative as those for Ca -ATPase. The reader is referred to Section 6.4.2 for further discussion of the Ca -ATPase system. 

The amino acid sequences of the SERCA pumps and the Na+K+ ATPase share 30% identity and 65% sequence similarity, and their topology relative to the membrane is also the same. Thus it seems likely that the Na+K+ ATPase structure is similar to that of the SERCA pumps and that all P-type ATPase transporters share the same basic structure. 

Mocz, G., and Gibbons, I. R. (2001). Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases. Structure (Camb.) 9, 93-103. 

The nucleotide occupancy of the catalytic sites observed in the first crystal structure was exactly what Paul Boyer had predicted earlier in his binding-change model of cooperative catalysis (Boyer, 1993). Consequently, this first high-resolution structure of the Fj-ATPase immediately initiated a number of studies that ultimately led to the elucidation of the F -. TPase s rotational mechanism of cooperative catalysis. At the time, the F - ATPase structure represented the largest asymmetric structure solved to atomic resolution by x-ray crystallography, and this accomplishment, together with the visionary prediction of rotary catalysis, was subsequently awarded the 1997 Nobel prize in chemistry (to John Walker for the structure and Paul Boyer for the catalytic mechanism). However, whether the first (and many subsequent) structure (s) represented physiologically... 

Morsomme, R, and Boutry, M. (2000). The plant plasma membrane H+-ATPase Structure, function and regulation. Biochim. Biophys. Acta 1465,1-16. 

The membrane proteins with ATP-binding cassette (ABC) domains are complex ATP-dependent pumps. Each pump includes four major domains two domains span the membrane and two others contain ABC P-loop ATPase structures. The multidrug resistance proteins confer resistance on cancer cells by pumping chemotherapeutic drugs out of a cancer cell before the drugs can exert their effects. Another ABC domain protein is the cystic fibrosis transmembrane conductance regulator (CFTR), an ATP-gated chloride channel. Mutations in CFTR can result in cystic fihrosis. 

Bublitz, M., Poulsen, H., Morth, J. P., Nissen, P. (2010). In and out of the cation pumps P-type ATPase structure revisited. Current Opinion in Structural Biology, 20, 431—439. 

Pedersen, P.L. (2005) Transport ATPases structure, motors, mechanism and medicine a brief overview. Journal of Bioenergetics and Biomembranes, IT] (6), 349-357. 

Fig. 37. Interaction of residues ofthe e-subunit of EcFi-ATPase with the a- and p-subunits of Fo Fi-ATPase known from cross-linking studies and modeled by the bovine MFi-ATPase structure. Figure source Uhlin, Cox and Guss (1997) Crystal structure ofthe e subunit of the proton-translocating ATP synthase from Escherichia coli. Structure 5 1227.

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