Energy Coupling Factor-Type ABC Transporters for Vitamin Uptake in Prokaryotes

被引:35
作者
Erkens, Guus B.
Majsnerowska, Maria
ter Beek, Josy
Slotboom, Dirk Jan [1 ]
机构
[1] Univ Groningen, Dept Biochem, Groningen Biomol Sci & Biotechnol Inst, NL-9747 AG Groningen, Netherlands
关键词
LACTOBACILLUS-CASEI; MEMBRANE-PROTEINS; LACTOCOCCUS-LACTIS; STRUCTURAL BASIS; BINDING; MECHANISM; THIAMINE; SEQUENCE; AFFINITY; SYSTEMS;
D O I
10.1021/bi300504v
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Energy coupling factor (ECF) transporters are a subgroup of ATP-binding cassette (ABC) transporters involved in the uptake of vitamins and micronutrients in prokaryotes. In contrast to classical ABC importers, ECF transporters do not make use of water-soluble substrate binding proteins or domains but instead employ integral membrane proteins for substrate binding (named S-components). S-components form active translocation complexes with the ECF module, an assembly of two nucleotide-binding domains (NBDs, or EcfA) and a second transmembrane protein. In some cases, the ECF module is dedicated to a single S-component, but in many cases, the ECF module can interact with several different S-components that are unrelated in sequence and bind diverse substrates. The modular organization with exchangeable S-components on a single ECF module allows the transport of chemically different substrates via a common route. The recent determination of the crystal structures of the S-components that recognize thiamin and riboflavin has provided a first clue about the mechanism of S-component exchange. This review describes recent advances and the current views of the mechanism of transport by ECF transporters.
引用
收藏
页码:4390 / 4396
页数:7
相关论文
共 42 条
[1]   Trends in protein evolution inferred from sequence and structure analysis [J].
Aravind, L ;
Mazumder, R ;
Vasudevan, S ;
Koonin, EV .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2002, 12 (03) :392-399
[2]   ABC transporter architecture and regulatory roles of accessory domains [J].
Biemans-Oldehinkel, E ;
Doeven, MK ;
Poolman, B .
FEBS LETTERS, 2006, 580 (04) :1023-1035
[3]   The riboflavin transporter RibU in Lactococcus lactis:: Molecular characterization of gene expression and the transport mechanism [J].
Burgess, CM ;
Slotboom, DJ ;
Geertsma, ER ;
Duurkens, RH ;
Poolman, B ;
van Sinderen, D .
JOURNAL OF BACTERIOLOGY, 2006, 188 (08) :2752-2760
[4]   A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle [J].
Chen, J ;
Lu, G ;
Lin, J ;
Davidson, AL ;
Quiocho, FA .
MOLECULAR CELL, 2003, 12 (03) :651-661
[5]   The ABC of ABCs: a phylogenetic and functional classification of ABC systems in living organisms [J].
Dassa, E ;
Bouige, P .
RESEARCH IN MICROBIOLOGY, 2001, 152 (3-4) :211-229
[6]   Structure, function, and evolution of bacterial ATP-binding cassette systems [J].
Davidson, Amy L. ;
Dassa, Elie ;
Orelle, Cedric ;
Chen, Jue .
MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 2008, 72 (02) :317-364
[7]  
Doolittle RF, 1986, Of URFs and ORFs: a primer on how to analyze derived amino acid sequences
[8]   Flavin binding to the high affinity riboflavin transporter RibU [J].
Duurkens, Ria H. ;
Tol, Menno B. ;
Geertsma, Eric R. ;
Permentier, Hjalmar P. ;
Slotboom, Dirk Jan .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (14) :10380-10386
[9]   The structural basis of modularity in ECF-type ABC transporters [J].
Erkens, Guus B. ;
Berntsson, Ronnie P-A ;
Fulyani, Faizah ;
Majsnerowska, Maria ;
Vujicic-Zagar, Andreja ;
ter Beek, Josy ;
Poolman, Bert ;
Slotboom, Dirk Jan .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2011, 18 (07) :755-U23
[10]   Biochemical Characterization of ThiT from Lactococcus lactis: A Thiamin Transporter with Picomolar Substrate Binding Affinity [J].
Erkens, Guus B. ;
Slotboom, Dirk Jan .
BIOCHEMISTRY, 2010, 49 (14) :3203-3212