Download ABC Proteins. From Bacteria to Man by I Barry Holland,Susan P. C. Cole,Karl Kuchler, et PDF

By I Barry Holland,Susan P. C. Cole,Karl Kuchler, et al.Elsevier|Elsevier Science||Academic PressAdult NonfictionScienceLanguage(s): EnglishOn sale date: 13.10.2011Street date: 07.01.2003

ABC Proteins is an in-depth, updated research of all that's recognized in regards to the topic up to now. It discusses and compares evolution, biology and mechanism of motion of all recognized ABC proteins, together with the 1st structural experiences in addition to medical implications. it is going to be precious to someone attempting to remain abreast of the newest findings. This ebook is bound to develop into a vintage and may usually be updated.

Key Features

  • Phylogeny and Evoloution of ABC Transporters
  • Fundamental elements of the Mechanism of motion of ABC Transporters
  • Prokaryote ABC Transporters
  • Non-Mammalian Transporters
  • Multidrug Transporters
  • ABC Transporters, Physiological Roles and Human Disease
  • Full colour all through
  • Show description

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    Proc. Natl Acad. Sci. USA. 1984;81:7333–7337. F. Structural and functional relationships of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport. Nature. 1990;346:362–365. F. The ABC (ATP-binding cassette) transporters of Escherichia coli. Mol. Microbiol. 1998;28:5–13. C. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science. 2002;296:1091–1098. , Callaghan R. The vinblastine binding site adopts high and low affinity conformations during the transport cycle of P-glycoprotein.

    INTRODUCTION ATP-binding cassette (ABC) systems constitute one of the most abundant families of proteins. At the time of writing this review, we have identified more than 2000 ABC ATPase domains or proteins in translated nucleic acid sequence databases. A total of about 6000 proteins were found when the partners of ATPases were taken into account. The size of this mass of sequences is therefore similar to the coding capacity of a bacterial genome. , 1988; Holland and Blight, 1999). The most prominent characteristic of these systems is that they share a highly conserved ATPase domain, the ABC, which has been demonstrated to bind and hydrolyze ATP, thereby providing energy for a large number of biological processes.

    L. Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport. Proc. Natl Acad. Sci. USA. 1989;86:6953–6957. J. Cysteine-scanning mutagenesis provides no evidence for the extracellular accessibility of the nucleotide-binding domains of the multidrug resistance transporter P-glycoprotein. EMBO J. 1999;23:6800–6808. B. Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters.

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