A common mechanism for ATP hydrolysis in ABC transporter and helicase superfamilies

被引:74
作者
Geourjon, C
Orelle, C
Steinfels, E
Blanchet, C
Deléage, G
Di Pietro, A
Jault, JM
机构
[1] Univ Lyon 1, Lab Bioinformat & RMN Struct, Inst Biol & Chim Prot, UMR 5086 CNRS, Lyon 07, France
[2] Univ Lyon 1, Lab Prot Resistance Agents Chimiotherapeut, Inst Biol & Chim Prot, UMR 5086 CNRS, Lyon 07, France
基金
澳大利亚研究理事会;
关键词
D O I
10.1016/S0968-0004(01)01907-7
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
ABC (ATP-binding cassette) transporters and helicases are large superfamilies of seemingly unrelated proteins, whose functions depend on the energy provided by ATP hydrolysis. Comparison of the 3D structures of their nucleotide-binding domains reveals that, besides two well-characterized ATP-binding signatures, the folds of their nucleotide-binding sites are similar. Furthermore, there are striking similarities in the positioning of residues thought to be important for ATP binding or hydrolysis. Interestingly, structures have recently been obtained for two ABC proteins that are not involved in transport activities, but that have a function related to DNA modification. These ABC proteins, which contain a nucleotide-binding site akin to those of typical ABC transporters, might constitute the missing link between the two superfamilies.
引用
收藏
页码:539 / 544
页数:6
相关论文
共 49 条
[1]   STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].
ABRAHAMS, JP ;
LESLIE, AGW ;
LUTTER, R ;
WALKER, JE .
NATURE, 1994, 370 (6491) :621-628
[2]   SPATIAL PRECISION OF A CATALYTIC CARBOXYLATE OF F1-ATPASE BETA-SUBUNIT PROBED BY INTRODUCING DIFFERENT CARBOXYLATE-CONTAINING SIDE-CHAINS [J].
AMANO, T ;
TOZAWA, K ;
YOSHIDA, M ;
MURAKAMI, H .
FEBS LETTERS, 1994, 348 (01) :93-98
[3]  
AMES GF, 1992, ADV ENZYMOL RAMB, V65, P1
[4]   Conserved domains in DNA repair proteins and evolution of repair systems [J].
Aravind, L ;
Walker, DR ;
Koonin, EV .
NUCLEIC ACIDS RESEARCH, 1999, 27 (05) :1223-1242
[5]   Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae -: the prototype of the DEAD box protein family [J].
Benz, J ;
Trachsel, H ;
Baumann, U .
STRUCTURE, 1999, 7 (06) :671-679
[6]   Complete inventory of the yeast ABC proteins [J].
Decottignies, A ;
Goffeau, A .
NATURE GENETICS, 1997, 15 (02) :137-145
[7]   Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis [J].
Diederichs, K ;
Diez, J ;
Greller, G ;
Müller, C ;
Breed, J ;
Schnell, C ;
Vonrhein, C ;
Boos, W ;
Welte, W .
EMBO JOURNAL, 2000, 19 (22) :5951-5961
[8]   Site-directed mutagenesis of motif III in PcrA helicase reveals a role in coupling ATP hydrolysis to strand separation [J].
Dillingham, MS ;
Soultanas, P ;
Wigley, DB .
NUCLEIC ACIDS RESEARCH, 1999, 27 (16) :3310-3317
[9]   ROLE OF GLUTAMINE-61 IN THE HYDROLYSIS OF GTP BY P21(H-RAS) - AN EXPERIMENTAL AND THEORETICAL-STUDY [J].
FRECH, M ;
DARDEN, TA ;
PEDERSEN, LG ;
FOLEY, CK ;
CHARIFSON, PS ;
ANDERSON, MW ;
WITTINGHOFER, A .
BIOCHEMISTRY, 1994, 33 (11) :3237-3244
[10]   ANTHEPROT-2.0 - A 3-DIMENSIONAL MODULE FULLY COUPLED WITH PROTEIN-SEQUENCE ANALYSIS-METHODS [J].
GEOURJON, C ;
DELEAGE, G .
JOURNAL OF MOLECULAR GRAPHICS, 1995, 13 (03) :209-212