ABC transporter: Difference between revisions

Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
Line 1: Line 1:
<StructureSection load='1l7v' size='400' side='right' scene='ABC_transporter/Cv/1' caption='Se-Met B12 Bacterial ABC Transporter complex with cyclo-tetrametavanadate, [[1l7v]].  Permease protein in green and grey,  ATP-binding protein in yellow and pink.'>
<StructureSection load='1l7v' size='400' side='right' scene='ABC_transporter/Cv/1' caption='Se-Met B12 Bacterial ABC Transporter complex with cyclo-tetrametavanadate, [[1l7v]].  Permease protein in green and grey,  ATP-binding protein in yellow and pink.'>


'''A'''TP '''B'''inding '''C'''assette (ABC) '''[[Transporters]]''' are ATP-dependent membrane proteins critical for most aspects of cell physiology, including the uptake of nutrients (importers) and elimination of waste products and energy generation (exporters) which are predominantly expressed in excretory organs, such as the liver, intestine, blood-brain barrier, blood-testes barrier, placenta, and kidney<ref name="Kidney"/><ref name="FourDomainsABCT"/>. There are many ABC Transporters in organisms, for instance, there are 28 in Saccharomyces,58 in Caenorhabditis, 51 in Drosophila,129 in Arabadopsis,and the 69 ABC transporters in E. coli account for almost 5% of its genomic coding capacity<ref name="EColi"/>. ABC transporter protein translocates substrates across membranes.  It contains a Solute Binding Domain (SBD).  CFTR (Cystic Fibrosis Transmembrane Regulator)  translocates chloride and  thiocyanate.  It contains a nucleotide binding domain (NBD).  Mutations in CFTR lead to Cystic Fibrosis. In humans the ABC transporters are classified into subfamilies, i.e. ABCB6 is ABC subfamily B member 6. The images at the left and at the right correspond to one representative ABC transporter, ''i.e.'' the crystal structure of B12 Bacterial ABC Transporter ([[1l7v]]).
'''A'''TP '''B'''inding '''C'''assette (ABC) '''[[Transporters]]''' are ATP-dependent membrane proteins critical for most aspects of cell physiology, including the uptake of nutrients (importers) and elimination of waste products and energy generation (exporters) which are predominantly expressed in excretory organs, such as the liver, intestine, blood-brain barrier, blood-testes barrier, placenta, and kidney<ref name="Kidney"/><ref name="FourDomainsABCT"/>. There are many ABC Transporters in organisms, for instance, there are 28 in Saccharomyces,58 in Caenorhabditis, 51 in Drosophila,129 in Arabadopsis,and the 69 ABC transporters in ''E. coli'' account for almost 5% of its genomic coding capacity<ref name="EColi"/>. ABC transporter protein translocates substrates across membranes.  It contains a Solute Binding Domain (SBD).  CFTR (Cystic Fibrosis Transmembrane Regulator)  translocates chloride and  thiocyanate.  It contains a nucleotide binding domain (NBD).  Mutations in CFTR lead to Cystic Fibrosis. In humans the ABC transporters are classified into subfamilies, i.e. ABCB6 is ABC subfamily B member 6. The images at the left and at the right correspond to one representative ABC transporter, ''i.e.'' the crystal structure of B12 Bacterial ABC Transporter ([[1l7v]]).


== Function ==
== Function ==
Line 10: Line 10:


To achieve export, ABC transporters require a minimum of four domains. Two transmembrane domains (TMDs) form the ligand binding sites and provide specificity, and two NBDs bind and hydrolyze ATP to drive the trans-location of the bound ligand. The NBDs, but not the TMDs, are homologous throughout the family and have several characteristic motifs including the Walker A and B motifs common to many nucleotide binding proteins and others like the ABC signature, stacking aromatic D, H, and Q loops, which are unique to the family<ref name="FourDomainsABCT"/>.
To achieve export, ABC transporters require a minimum of four domains. Two transmembrane domains (TMDs) form the ligand binding sites and provide specificity, and two NBDs bind and hydrolyze ATP to drive the trans-location of the bound ligand. The NBDs, but not the TMDs, are homologous throughout the family and have several characteristic motifs including the Walker A and B motifs common to many nucleotide binding proteins and others like the ABC signature, stacking aromatic D, H, and Q loops, which are unique to the family<ref name="FourDomainsABCT"/>.
== Disease ==
There are currently 50 known ABC transporters in human.  Of these there are 13 genetic diseases known to be associated with 14 of them.  Among the diseases are cystic fibrosis, Stargardt disease, age-related macular degeneration and others.
</StructureSection>
</StructureSection>


Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Zina Saadi, Alexander Berchansky, Michal Harel, Joel L. Sussman