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GalP (protein)
The galactose permease or GalP found in ''Escherichia coli'' is an integral membrane protein involved in the transport of monosaccharides, primarily hexoses, for utilization by ''E. coli'' in glycolysis and other metabolic and catabolic pathways (3,4). It is a member of the Major Facilitator Super Family (MFS) and is homologue of the human GLUT1 transporter (4). Below you will find descriptions of the structure, specificity, effects on homeostasis, expression, and regulation of GalP along with examples of several of its homologues.
==Structure==
Galactose Permease (GalP), is a member of the Major Facilitator Super Family (MFS) and therefore has structural similarities to the other members of this super family such as GLUT1 (4). All members of the MFS have 12 membrane spanning alpha(α)-helices with both the C- and N-termini located on the cytoplasmic side of the membrane (4). Figure 1a (3) depicts how the 12 helices are divided into two halves, that are pseudo-symmetric, of 6 helices which are attached by a long hydrophilic cytoplasmic loop between helix 6 and helix 7 (2,3,4). These two halves come together to form a pore for substrate transport, in GalP, the substrates are primarily galactose, glucose, and H+. GalP monomers have a pore of approximately 10Å in diameter, which is consistent with the pore sizes found in other members of the MFS, between 10-15Å (4). GalP has been found as an oligomer formed by a homotrimer of GalP monomers that exhibits p3 or 3-fold rotational symmetry (Figure 1b-c) (4). GalP is the first member of the MFS that has been found as a trimer and to be biologically active in its trimeric form; it is thought that the GalP oligomer is formed for stability (4).
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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