By John N. Abelson, Melvin I. Simon, Suresh V. Ambudkar, Michael M. Gottesman
The significantly acclaimed laboratory typical for greater than 40 years, Methods in Enzymology is likely one of the so much hugely revered courses within the box of biochemistry. on account that 1955, each one quantity has been eagerly awaited, usually consulted, and praised by means of researchers and reviewers alike. greater than 285 volumes were released (all of them nonetheless in print) and masses of the fabric is correct even today-truly a necessary e-book for researchersin all fields of existence sciences.
* Prokaryotic ABC Transporters
* Eukaryotic ABC Transporters
* Nonmammalian ABC delivery Systems
* Mammalian P-Glycoproteins
* Multidrug Resistance linked Protein
* Cystic Fibrosis Transmembrane Conductance Regulator
* Sulfonylurea Receptor
* Intracellular ABC Transporters
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Extra info for ABC Transporters: Biochemical, Cellular, and Molecular Aspects
Williams and T. Ferenci, J. BacterioL 163, 1237 (1985). ~3A. L. Davidson, S. S. Laghaeian, and D. E. Mannering, J. Biol. Chem. 271, 4858 (1996). 84j. p. Abrahams, A. G. W. Leslie, R. Luner, and J. E. Walker, Nature 370, 621 (1994). 18 PROKARYOTIC ABC TRANSPORTERS [11 of the possible presence of closed conformers among ligand-free MBP molecules. Interesting results were obtained when the A T P hydrolysis assay was performed by using proteoliposomes containing MBP-independent mutants of rnalF and m a l G .
Microbiol. 5, 1375 (1991). 3~ S. C. Hyde, P. Emsley, M. J. Hartshorn, M. M. Mimmack, U. Gileadi, S. R. Pearce, M. P. Gallagher, D. R. Gill, R. E. Hubbard, and C. Higgins, Nature 345, 362 (1990). 39 C. S. Mimura, S. R. Holbrook, and G. -L. A m e s , Proc. NatL Acad. Sci. USA 88, 84 (1991). 10 PROKARYOTIC ABC TRANSPORTERS [11 The N-terminal part containing the Walker motif A and the C-terminal part containing the Walker motif B (Fig. 1) are predicted to fold together in a way similar to the model protein and to produce the ATP-binding pocket, but the large, middle part of the protein containing about 90 amino acid residues was excluded entirely from this pocket structure in at least one model.
These mutants are altered in the integral m e m b r a n e proteins MalF or MalG, and transport maltose specifically. The affinity for maltose, however, is much lower, and the transport Km for maltose is about 1 raM, in contrast to the transport Kin, about 1/xM, of the wild-type transport system that includes MBP. All MBP-independent mutants contain two mutations either in m a l F or m a l G . One of them occurs in the "distal" region, predicted to be buried deep in the m e m b r a n e interior, and the other occurs in the " p r o x i m a l " region, close to the periplasmic surface of the protein.
ABC Transporters: Biochemical, Cellular, and Molecular Aspects by John N. Abelson, Melvin I. Simon, Suresh V. Ambudkar, Michael M. Gottesman