STR2
ATP-binding cassette transporters ( ABC-transporter ) are transmembrane proteins that utilize the energy of adenosine triphosphate (ATP) hydrolysis to carry out certain biological processes including translocation of various substrates across membranes and non-transport-related processes such as translation of RNA and DNA repair.
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Annotated Information
Function
Bacterial ABC importers are essential in cell viability, virulence and pathogenicity. Other than functioning in transport, some bacterial ABC proteins are also involved in the regulation of several physiological processes. In bacterial efflux systems, certain substances include surface components of the bacterial cell, proteins involved in bacterial pathogenesis and so on. They also play important roles in biosynthetic pathways[1].Human ABC transporters are involved in several diseases that arise from polymorphisms in ABC genes and rarely due to complete loss of function of single ABC proteins. More recently, ABC-transporters have been shown to exist within the placenta[2].
Structure
Transmembrane domain (TMD): also known as membrane-spanning domain (MSD) or integral membrane (IM) domain, consists of alpha helices, embedded in the membrane bilayer. NBD(nucleotide-binding domain) or ATPbinding cassette (ABC) domain, on the other hand, is located in the cytoplasm and has a highly conserved sequence. The structural architecture of ABC transporters consists minimally of two TMDs and two ABCs. Four individual polypeptide chains including two TMD and two NBD subunits, may combine to form a full transporter. Most exporters are made up of a homodimer consisting of two half transporters or monomers of a TMD fused to a nucleotide-binding domain (NBD). Some ABC transporters have additional elements.
Methods
relatively simple membrane assays like vesicular transport assay, ATPase assay, more complex cell based assays, intricate in vivo detection methodologies
Labs working on this gene
References
- ↑ Sippel KH1, Bacik J2, Quiocho FA1, Fisher SZ3. Acta Crystallogr F Struct Biol Commun. 2014 Jun 1;70(Pt 6):819-822. Epub 2014 May 25.
- ↑ Sugiyama S1, Kashiwagi K2, Kakinouchi K1, Tomitori H2, Kanai K2, Murata M1, Adachi H3, Matsumura H3, Takano K3, Murakami S3, Inoue T3, Mori Y3, Igarashi K4. Plant CActa Crystallogr F Struct Biol Commun. 2014 Jun 1;70(Pt 6):738-741. Epub 2014 May 10.ell Reports, 2012, 31(7): 1333-1343