ATP-binding proteins

Approximately 500 of the 820 amino acid residues of the myosin head are highly conserved between various species. One conserved region, located approximately at residues 170 to 214, constitutes part of the ATP-binding site. Whereas many ATP-binding proteins and enzymes employ a /3-sheet-a-helix-/3-sheet motif, this region of myosin forms a related a-f3-a structure, beginning with an Arg at (approximately) residue 192. The /3-sheet in this region of all myosins includes the amino acid sequence... 

Hyde, S.C., Emsley, P., Hartshorn, M.J., Mimmack, M.M., Gileadi, U., Pearce, S. R., Gallagher, M.P., Gill, D.R., Hubbard, R.E. and Higgins, C.F. (1990) Structural model of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport. Nature, 346, 362-365. 

Flavonoids are known to inhibit the function of many ATP-binding proteins, such as mitochondrial ATPase, myosin, Na/K and Ca plasma membrane ATPases, protein kinases, topoisomerase II, and multidrug resistance (MDR) proteins. In general, inhibition takes place through binding of the flavonoids to the ATP-binding site. Only two cases relevant to the inhibition of carcinogenesis by flavonoids" " will be discussed in detail. 

ATP-binding proteins involved in active transport (ABC transporters) DNA and RNA helicases... 

Harata NC, Aravanis AM, Tsien,R (2006) Kiss-and-run and full-collapse fusion as modes of exo-endocytosis in neurosecretion. J Neurochem 97 1546-70 Hosaka M, Stidhof TC (1998) Synapsins I and II are ATP-binding proteins with differential Ca2+ regulation. J Biol Chem 273 1425-9 Jahn R, Lang T, Stidhof TC (2003) Membrane fusion. Cell 112 519-33... 

Hosaka M, Siidhof TC (1998) Synapsins I and II are ATP-binding proteins with differential Ca2+ regulation. J Biol Chem 273 1425-9... 

Figure 5-8. Photoafifinity labelling of ATP binding proteins with 8-azido-ATP. Irradiation of the 8-azido-ATP bound to the protein releases nitrogen and forms a highly reactive nitrene radical...

Key words ATP-binding proteins, Drug design, Drug discovery, Purinome... 

F. 7.9. G-Actin. ATP binds in the center of the cleft. The two domains that form the cleft are further subdivided into subdomains 1-4. The overall structure is found in many ATP-binding proteins and is called the actin fold. The conformations of the regions shown in blue are nearly superimposable among the proteins that contain the actin fold. (From Kabsch W, Holmes KC. The actin fold. FASEB J 1995 9 167-174.)... 

A Oligopeptide permease B Oligopeptide transport ATP binding protein or Oligopeptide permease C Hypothetical protien D Hypothetical protein E Hypothetical protein F Phosphomannomutase G ABC transporter. 

ABC transporter proteins are a ubiquitous family of proteins characterised by an ATP-binding cassette (ABC) motif (Chapter 42). These ATP-binding proteins belong to one of the largest families known to medical science. The bound ATP is hydrolysed in a process coupled to transport of their substrate. One such protein is the cholesterol transporter known as ABC-Al (not shown in Fig. 41.1). It is found in many tissues where its function is to transfer excess cholesterol to HDL particles. The HDL particles proceed to the liver for disposal. 

Incubate on heating block for 30-90 min at 37°C (depending on the GDP exchange kinetics of the protein to be labeled). For labeling of ATP-binding proteins a 5-min incubation is sufficient. 

G) Energy ATP synthase, mitochondrial ATP-binding protein ATPase... 

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