ABC Transporters: Biochemical, Cellular, and Molecular by John N. Abelson, Melvin I. Simon, Suresh V. Ambudkar, PDF

By John N. Abelson, Melvin I. Simon, Suresh V. Ambudkar, Michael M. Gottesman

ISBN-10: 0076687929

ISBN-13: 9780076687923

ISBN-10: 0121821935

ISBN-13: 9780121821937

The significantly acclaimed laboratory common for greater than 40 years, Methods in Enzymology is without doubt one of the such a lot hugely revered guides within the box of biochemistry. because 1955, every one quantity has been eagerly awaited, often consulted, and praised via researchers and reviewers alike. greater than 285 volumes were released (all of them nonetheless in print) and lots more and plenty of the cloth is appropriate even today-truly an important book for researchersin all fields of lifestyles sciences.

Key Features
* Prokaryotic ABC Transporters
* Eukaryotic ABC Transporters
* Nonmammalian ABC shipping Systems
* Mammalian P-Glycoproteins
* Multidrug Resistance linked Protein
* Cystic Fibrosis Transmembrane Conductance Regulator
* Sulfonylurea Receptor
* Intracellular ABC Transporters

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Additional resources for ABC Transporters: Biochemical, Cellular, and Molecular Aspects

Example text

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. 39 This portion, often called the helical d o m a i n , and a linker region that connects the C-terminal end of the helical domain to the ATPase portion of the molecule (Fig. 1) are hypothesized to be important in coupling A T P hydrolysis to conformational changes in the channel portion of the transporter, u Interestingly, several mutations in HisP that uncouple A T P hydrolysis from solute translocation are indeed located in this linker region as well as at the beginning of the second ATP-binding region, a° Some of the ATP-binding subunits apparently perform additional functions.

A. Shuman and co-workers, 52 of E. coli mutants that no longer require the presence of M B P for the transport of maltose. 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 .

Shuman, J. Mol. Biol. 233, 659 (1993). [11 BACTERIALABC TRANSPORTERS 13 ABC transporters, possibly their channel domains, and the helper proteins (see Table I) play no role in the specificityF Recently, random mutagenesis of helices 6, 7, and 8 of MalF was carried out by Ehrle et aL 58 Many mutations, clustered on one face of helix 6, changed the specificity of transport, again showing that the channel protein contributes to substrate specificity. Many of them transported maltoheptaose but not maltose.

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ABC Transporters: Biochemical, Cellular, and Molecular Aspects by John N. Abelson, Melvin I. Simon, Suresh V. Ambudkar, Michael M. Gottesman

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