ATP-binding domain of ABC transporters


ATP-binding domain of ABC transporters

Pfam_box
Symbol = ABC_tran
Name =


width =
caption =Multidrug ABC transporter SAV1866, closed state
Pfam= PF00005
InterPro= IPR003439
SMART=
PROSITE = PDOC00185
SCOP = 1b0u
TCDB = 3.A.1
OPM family= 17
OPM protein=2hyd
PDB=PDB3|1vplA:29-210 PDB3|1g9xA:33-229 PDB3|1g6hA:33-229PDB3|1gajA:33-229 PDB3|1ji0A:31-214 PDB3|1z47A:29-210PDB3|2awnA:29-210 PDB3|1q1bD:29-210 PDB3|1q12A:29-210PDB3|2awoC:29-210 PDB3|1q1eA:29-210 PDB3|1vciA:38-219PDB3|1v43A:38-219 PDB3|1g292:29-216 PDB3|1oxsC:31-217PDB3|1oxvA:31-217 PDB3|1oxtA:31-217 PDB3|1oxuC:31-217PDB3|1oxxK:31-217 PDB3|1b0uA:32-229 PDB3|1f3oA:31-221PDB3|1l2tA:31-221 PDB3|1l7vC:26-209 PDB3|1z2rG:369-554PDB3|1pf4D:369-554 PDB3|2ap2P:1103-1116 PDB3|1mv5A:375-560PDB3|1xefC:495-679 PDB3|1mt0A:495-679 PDB3|1jj7A:531-718PDB3|1ckwA:497-522 PDB3|1ckxA:497-522 PDB3|1ckyA:497-522PDB3|1ckzA:497-522 PDB3|1xmiB:451-622 PDB3|2bbsA:451-622PDB3|2bbtA:451-622 PDB3|1nbd :451-622 PDB3|1xmjA:451-622PDB3|2bboA:451-622 PDB3|1r0wD:451-622 PDB3|1xfaA:451-622PDB3|1r0xB:451-622 PDB3|1r0zB:451-622 PDB3|1q3hD:451-622PDB3|1xf9B:451-622 PDB3|1r0yA:451-622 PDB3|1r10A:451-622PDB3|1yqtA:99-286 PDB3|1sgwA:27-190 PDB3|2d3wA:27-222PDB3|2d2fA:29-220 PDB3|2d2eA:29-220

ATP-binding domain of ABC transporters is a water-soluble domain of transmembrane ABC transporters.

ABC transporters belong to the ATP-Binding Cassette superfamily, which uses the hydrolysis of ATP to translocate a variety of compounds across biological membranes. ABC transporters are minimally constituted of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These regions can be found on the same protein or on two different ones. Most ABC transporters function as a dimer and therefore are constituted of four domains, two ABC modules and two TMDs.

Biological function

ABC transporters are involved in the export or import of a wide variety of substrates ranging from small ions to macromolecules. The major function of ABC import systems is to provide essential nutrients to bacteria. They are found only in prokaryotes and their four constitutive domains are usually encoded by independent polypeptides (two ABC proteins and two TMD proteins). Prokaryotic importers require additional extracytoplasmic binding proteins (one or more per systems) for function. In contrast, export systems are involved in the extrusion of noxious substances, the export of extracellular toxins and the targeting of membrane components. They are found in all living organisms and in general the TMD is fused to the ABC module in a variety of combinations. Some eukaryotic exporters encode the four domains on the same polypeptide chain.

Amino acid sequence

The ABC module (approximately two hundred amino acid residues) is known to bind and hydrolyze ATP, thereby coupling transport to ATP hydrolysis in a large number of biological processes. The cassette is duplicated in several subfamilies. Its primary sequence is highly conserved, displaying a typical phosphate-binding loop: Walker A, and a magnesium binding site: Walker B. Besides these two regions, three other conserved motifs are present in the ABC cassette: the switch region which contains a histidine loop, postulated to polarize the attacking water molecule for hydrolysis, the signature conserved motif (LSGGQ) specific to the ABC transporter, and the Q-motif (between Walker A and the signature), which interacts with the gamma phosphate through a water bond. The Walker A, Walker B, Q-loop and switch region form the nucleotide binding site.

3D structure

The 3D structure of a monomeric ABC module adopts a stubby L-shape with two distinct arms. ArmI (mainly beta-strand) contains Walker A and Walker B. The important residues for ATP hydrolysis and/or binding are located in the P-loop. The ATP-binding pocket is located at the extremity of armI. The perpendicular armII contains mostly the alpha helical subdomain with the signature motif. It only seems to be required for structural integrity of the ABC module. ArmII is in direct contact with the TMD. The hinge between armI and armII contains both the histidine loop and the Q-loop, making contact with the gamma phosphate of the ATP molecule. ATP hydrolysis leads to a conformational change that could facilitate ADP release. In the dimer the two ABC cassettes contact each other through hydrophobic interactions at the antiparallel beta-sheet of armI by a two-fold axis.

Human proteins containing this domain

ABCA1; ABCA10; ABCA12; ABCA13; ABCA2; ABCA3; ABCA4; ABCA5;
ABCA6; ABCA7; ABCA8; ABCA9; ABCB1; ABCB10; ABCB11; ABCB4;
ABCB5; ABCB6; ABCB7; ABCB8; ABCB9; ABCC1; ABCC10; ABCC11;
ABCC12; ABCC2; ABCC3; ABCC4; ABCC5; ABCC6; ABCC8; ABCC9;
ABCD1; ABCD2; ABCD3; ABCD4; ABCE1; ABCF1; ABCF2; ABCF3;
ABCG1; ABCG2; ABCG4; ABCG5; ABCG8; CFTR; MRP3; TAP1;
TAP2; TAPL;

References

* [1] Homology between proteins controlling Streptomyces fradiae tylosin resistance and ATP-binding transport. Rosteck PR Jr, Reynolds PA, Hershberger CL; Gene 1991;102:27-32. PMID|1864505
* [2] Structure and function of haemolysin B,P-glycoprotein and other members of a novel family of membrane translocators. Blight MA, Holland IB; Mol Microbiol 1990;4:873-880. PMID|1977073
* [3] Binding protein-dependent transport systems. Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher MP; J Bioenerg Biomembr 1990;22:571-592. PMID|2229036
* [4] Crystal structure of the ATP-binding subunit of an ABC transporter. Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH; Nature 1998;396:703-707. PMID|9872322


Wikimedia Foundation. 2010.

Look at other dictionaries:

  • Transmembrane domain of ABC transporters — Pfam box Symbol = ABC membrane Name = ABC transporter transmembrane region width = caption = Pfam= PF00664 InterPro= IPR001140 SMART= PROSITE = PDOC00364 SCOP = 1pf4 TCDB = 3.A.1 OPM family= 18 OPM protein= 1pf4 PDB=ABC transporter transmembrane… …   Wikipedia

  • ATP-binding cassette transporter — ATP binding cassette transporters (ABC transporter) are members of a superfamily that is one of the largest, and most ancient families with representatives in all extant phyla from prokaryotes to humans. Ref|Jones2004. These are transmembrane… …   Wikipedia

  • ATP-binding cassette family — The ATP binding cassette (ABC) family is a group of proteins which bind and hydrolyse ATP in order to transport substances across cellular membranes. They are prevalent in bacteria but are also in humans, and responsible for a diverse range of… …   Wikipedia

  • Protein domain — Pyruvate kinase, a protein from three domains (PDB 1pkn) A protein domain is a part of protein sequence and structure that can evolve, function, and exist independently of the rest of the protein chain. Each domain forms a compact three… …   Wikipedia

  • TAP2 — Transporter 2, ATP binding cassette, sub family B (MDR/TAP), also known as TAP2, is a human gene. PBB Summary section title = summary text = The membrane associated protein encoded by this gene is a member of the superfamily of ATP binding… …   Wikipedia

  • ABCD1 — is a protein that transfers fatty acids into peroxisomes. A deficiency is associated with adrenoleukodystrophy. PBB Summary section title = summary text = The protein encoded by this gene is a member of the superfamily of ATP binding cassette… …   Wikipedia

  • SMC protein — SMC proteins represent a large family of ATPases that participate in many aspects of higher order chromosome organization and dynamics.cite journal |author=Hirano T|title=The ABCs of SMC proteins: two armed ATPases for chromosome condensation,… …   Wikipedia

  • P-glycoprotein — ATP binding cassette, sub family B (MDR/TAP), member 1 Crystallographic structure of the mouse MDR3 protein. The approximate positioning of the protein in the cell membrane is indicated by the blue (extracellular face) and red (cytoplasmic face)… …   Wikipedia

  • Multidrug resistance-associated protein 2 — ATP binding cassette, sub family C (CFTR/MRP), member 2 Identifiers Symbols ABCC2; ABC30; CMOAT; DJS; KIAA1010; MRP2; cMRP External IDs …   Wikipedia

  • ABCA7 — ATP binding cassette, sub family A (ABC1), member 7, also known as ABCA7, is a human gene.cite web | title = Entrez Gene: ABCA7 ATP binding cassette, sub family A (ABC1), member 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene… …   Wikipedia


Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”

We are using cookies for the best presentation of our site. Continuing to use this site, you agree with this.