Transmembrane domain of ABC transporters
| ABC transporter transmembrane region | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | ABC_membrane | ||||||||
| Pfam | PF00664 | ||||||||
| InterPro | IPR001140 | ||||||||
| PROSITE | PDOC00364 | ||||||||
| SCOP | 1pf4 | ||||||||
| SUPERFAMILY | 1pf4 | ||||||||
| TCDB | 3.A.1 | ||||||||
| OPM superfamily | 17 | ||||||||
| OPM protein | 2hyd | ||||||||
| |||||||||
ABC transporter transmembrane domain is the main transmembrane structural unit of ATP-binding cassette transporter proteins, consisting of six alpha helixes that traverse the plasma membrane. Many members of the ABC transporter family (Pfam PF00005) have two such regions.[1][2][3][4][5][6]
Subfamilies
- Sulphate ABC transporter permease protein 2 InterPro: IPR005667
- Phosphate transport system permease protein 2 InterPro: IPR005672
- Phosphonate uptake transporter InterPro: IPR005769
- Nitrate transport permease InterPro: IPR005889
- NifC-like ABC-type porter InterPro: IPR006469
- Phosphate ABC transporter, permease protein PstC InterPro: IPR011864
- Molybdate ABC transporter, permease protein InterPro: IPR011867
- Nickel ABC transporter, permease subunit NikB InterPro: IPR014156
- Nickel ABC transporter, permease subunit NikC InterPro: IPR014157
- Ectoine/hydroxyectoine ABC transporter, permease protein EhuD InterPro: IPR014341
- Ectoine/hydroxyectoine ABC transporter, permease protein EhuC InterPro: IPR014342
Human proteins containing this domain
ABCB1; ABCB10; ABCB11; ABCB4; ABCB5; ABCB6; ABCB7; ABCB8; ABCB9; ABCC1; ABCC10; ABCC11; ABCC12; ABCC13; ABCC2; ABCC3; ABCC4; ABCC5; ABCC6; ABCC8; ABCC9; CFTR; TAP1; TAP2; TAPL;
References
- ↑ Kerr ID (2002). "Structure and association of ATP-binding cassette transporter nucleotide-binding domains". Biochim. Biophys. Acta. 1561 (1): 47–64. doi:10.1016/s0304-4157(01)00008-9. PMID 11988180.
- ↑ Hunt JF, Yuan YR, Martsinkevich O, Millen L, Thomas PJ, Karpowich N, Dai PL, MacVey K (2001). "Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter". Structure. 9 (7): 571–86. doi:10.1016/S0969-2126(01)00617-7. PMID 11470432.
- ↑ Hunt JF, Yuan YR, Blecker S, Martsinkevich O, Millen L, Thomas PJ (2001). "The crystal structure of the MJ0796ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter". J. Biol. Chem. 276 (34): 32313–21. doi:10.1074/jbc.M100758200. PMID 11402022.
- ↑ Kim SH, Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF (1998). "Crystal structure of the ATP-binding subunit of an ABC transporter". Nature. 396 (6712): 703–707. doi:10.1038/25393. PMID 9872322.
- ↑ Welte W, Breed J, Boos W, Diederichs K, Vonrhein C, Muller C, Diez J, Greller G, Schnell C (2000). "Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis". EMBO J. 19 (22): 5951–61. doi:10.1093/emboj/19.22.5951. PMC 305842. PMID 11080142.
- ↑ Wiley DC, Gaudet R (2001). "Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing". EMBO J. 20 (17): 4964–72. doi:10.1093/emboj/20.17.4964. PMC 125601. PMID 11532960.
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