ABC transporter-like, conserved site
Short name | ABC_transporter-like_CS |
Description
References
1.Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter. Karpowich N, Martsinkevich O, Millen L, Yuan YR, Dai PL, MacVey K, Thomas PJ, Hunt JF. Structure 9, 571-86, (2001). View articlePMID: 11470432
2.The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter. Yuan YR, Blecker S, Martsinkevich O, Millen L, Thomas PJ, Hunt JF. J. Biol. Chem. 276, 32313-21, (2001). View articlePMID: 11402022
3.ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains. Schneider E, Hunke S. FEMS Microbiol. Rev. 22, 1-20, (1998). View articlePMID: 9640644
4.Structure and association of ATP-binding cassette transporter nucleotide-binding domains. Kerr ID. Biochim. Biophys. Acta 1561, 47-64, (2002). View articlePMID: 11988180
5.ABC transporters: physiology, structure and mechanism--an overview. Higgins CF. Res. Microbiol. 152, 205-10, (2001). View articlePMID: 11421269
6.ABC transporters: from microorganisms to man. Higgins CF. Annu. Rev. Cell Biol. 8, 67-113, (1992). View articlePMID: 1282354
7.Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing. Gaudet R, Wiley DC. EMBO J. 20, 4964-72, (2001). View articlePMID: 11532960
8.The ABC of ABCS: a phylogenetic and functional classification of ABC systems in living organisms. Dassa E, Bouige P. Res. Microbiol. 152, 211-29, (2001). View articlePMID: 11421270
9.Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. Saurin W, Hofnung M, Dassa E. J. Mol. Evol. 48, 22-41, (1999). View articlePMID: 9873074
10.Domainal evolution of a prokaryotic DNA repair protein and its relationship to active-transport proteins. Doolittle RF, Johnson MS, Husain I, Van Houten B, Thomas DC, Sancar A. Nature 323, 451-3, (1986). View articlePMID: 3762695
11.Crystal structure of the ATP-binding subunit of an ABC transporter. Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH. Nature 396, 703-7, (1998). View articlePMID: 9872322
12.Binding protein-dependent transport systems. Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher MP. J. Bioenerg. Biomembr. 22, 571-92, (1990). View articlePMID: 2229036
13.Structure and function of haemolysin B,P-glycoprotein and other members of a novel family of membrane translocators. Blight MA, Holland IB. Mol. Microbiol. 4, 873-80, (1990). View articlePMID: 1977073
14.Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. Walker JE, Saraste M, Runswick MJ, Gay NJ. EMBO J. 1, 945-51, (1982). View articlePMID: 6329717
15.The P-loop--a common motif in ATP- and GTP-binding proteins. Saraste M, Sibbald PR, Wittinghofer A. Trends Biochem. Sci. 15, 430-4, (1990). View articlePMID: 2126155
16.A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria. Higgins CF, Hiles ID, Salmond GP, Gill DR, Downie JA, Evans IJ, Holland IB, Gray L, Buckel SD, Bell AW. Nature 323, 448-50, (1986). View articlePMID: 3762694
17.A family of closely related ATP-binding subunits from prokaryotic and eukaryotic cells. Higgins CF, Gallagher MP, Mimmack ML, Pearce SR. Bioessays 8, 111-6, (1988). View articlePMID: 3288195
18.Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. Diederichs K, Diez J, Greller G, Muller C, Breed J, Schnell C, Vonrhein C, Boos W, Welte W. EMBO J. 19, 5951-61, (2000). View articlePMID: 11080142
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
ENZYME
- 2.7.8.37
- 3.1.2.-
- 3.4.21.-
- 3.4.22.-
- 3.6.1.-
- 3.6.3.-
- 3.6.4.-
- 3.6.5.-
- 5.6.1.6
- 7.2.2.-
- 7.2.2.11
- 7.2.2.16
- 7.2.2.17
- 7.2.2.18
- 7.2.2.2
- 7.2.2.20
- 7.2.2.4
- 7.2.2.5
- 7.2.2.7
- 7.3.2.-
- 7.3.2.1
- 7.3.2.2
- 7.3.2.3
- 7.3.2.4
- 7.3.2.5
- 7.3.2.6
- 7.4.2.-
- 7.4.2.1
- 7.4.2.10
- 7.4.2.11
- 7.4.2.12
- 7.4.2.14
- 7.4.2.5
- 7.4.2.6
- 7.4.2.7
- 7.4.2.9
- 7.5.2.-
- 7.5.2.1
- 7.5.2.10
- 7.5.2.11
- 7.5.2.12
- 7.5.2.13
- 7.5.2.3
- 7.5.2.4
- 7.5.2.5
- 7.5.2.6
- 7.5.2.7
- 7.5.2.8
- 7.5.2.9
- 7.6.2.-
- 7.6.2.1
- 7.6.2.10
- 7.6.2.11
- 7.6.2.12
- 7.6.2.13
- 7.6.2.14
- 7.6.2.15
- 7.6.2.16
- 7.6.2.2
- 7.6.2.3
- 7.6.2.4
- 7.6.2.5
- 7.6.2.6
- 7.6.2.7
- 7.6.2.8
- 7.6.2.9
Contributing Member Database Entry
- PROSITE patterns:PS00211