ABC Proteins: From Bacteria to Man - download pdf or read online

By I Barry Holland, Susan P. C. Cole, Karl Kuchler, Christopher F. Higgins

ISBN-10: 0123525519

ISBN-13: 9780123525512

ABC Proteins is an in-depth, updated research of all that's identified concerning the topic thus far. It discusses and compares evolution, biology and mechanism of motion of all identified ABC proteins, together with the 1st structural reports in addition to medical implications. it is going to be precious to somebody attempting to remain abreast of the most recent findings. This e-book is bound to turn into a vintage and may on a regular basis be up to date. Key good points* Phylogeny and Evoloution of ABC Transporters* basic features of the Mechanism of motion of ABC Transporters* Prokaryote ABC Transporters* Non-Mammalian Transporters* Multidrug Transporters* ABC Transporters, Physiological Roles and Human illness* complete colour all through

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C, Oligopeptide importer (OPN family): two heterodimers of IMs and ABCs. D, Ferric-hydroxamate importer (ISVH subfamily): the two IM domains are fused in a single polypeptide chain. E, Ribose importer (MOS family): the two ABC domains are fused in a single polypeptide chain. F, Glutamine importer (PAO family): a homodimer of IM and a homodimer of ABC. , 1997). , 1999). The best-characterized system of this family, the E. coli maltose/maltodextrin transporter energized by MalK, is reviewed in Chapter 9.

D, Two types of proteins of the ABCA subfamily. The systems with an IM-ABC organization are found in completed genomes and none has been characterized. It is not known if they determine homo- or heterodimeric transporters. The ABCA1 and the ABCR proteins display an (IM-ABC)2 organization. , 1995). It has been proposed that the NodIJ system is a transporter that mediates the export of Nod factors. , 1996). , 1992). The NAT subfamily A transposition mutant of B. subtilis, isolated on the basis of growth inhibition by Naϩ at elevated pH, was found to be deficient in energydependent Naϩ extrusion.

The DRI family involved in drug resistance, and bacteriocin and lantibiotic immunity This family is composed of systems having the same global organization as those of the DRA family. 1). No significant similarity could be detected between IM proteins of these two families. DRI family systems are found in prokaryotes and some of these are involved in antibiotic resistance and in bacteriocin and lantibiotic immunity. The BAI subfamily involved in bacteriocin immunity Immunity towards bacteriocins such as lacticin RM, pediocin A and butyrivibriocin AR10 is conferred by transporters composed of one ABC and one IM.

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ABC Proteins: From Bacteria to Man by I Barry Holland, Susan P. C. Cole, Karl Kuchler, Christopher F. Higgins


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