Hypothetical protein Introduction: Difference between revisions

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'''Breif Introduction'''  
The sugars fucose and ribose both play an important role in the function of cells. Ribose is used in a range of cells for differing purposes, such as DNA, RNA synthesis and limited nutritional purposes. Fucose on the other hand plays an important role in cell receptors involved with cell to cell adhesion. Both of these sugars require transport systems to gain access into the cell.
These transport systems used are called ATP-cassette binding (ABC) systems. These ATP-binding cassette (ABC)-type systems have been found to mediate the uptake of solutes such as amino acids, peptides, ions, vitamins, and sugars in a wide range of bacteria (Tuner et al. 1999).These ABC transport systems are found in all forms of life, both eukaryotes and prokaryotes.
The structure of a typical prokaryote type ABC transporter consists of three types of components: two peripheral proteins that bind and hydrolyze ATP, two integral proteins each having six transmembrane segments  and a periplasmic substrate binding protein (Igarashi et al 2004).
 
The FucU/RbsD superfamily of proteins are involved with the transport of fucose and ribose into the cell. These proteins are thought to be involved with the anomeric conversion of these two sugars . RbsD proteins convert beta-purine ribose into its furine counterpart (see figure 1) which is needed for the next step in metabolism. FucU proteins on the other hand catalyze the change of alpha-purine fucose into the beta form (see figure 2). The beta form is needed for use in the salvage pathway to form a number of important receptors and secretions (Kim et al. 2003).
 
[[Image:sugar.jpg]]
 
''Figure 1.This shows the difference between the 5 ring franose and the six ring pruanose form of ribose. (Kim et al. 2003) ''  
 
 
[[Image:fuc.jpg]]
 
''Figure 2.This shows the difference between the alpha and beta form of fucose. (Ryu et al. 2007)''
   
The 2ob5A protein (Hypothetical protein LOC282969 isoform 1) is found to be a member of the FucU/RbsD superfamily. The aim of this report is to provide information covering the evolutionary history of the protein through the construction of a phylogenic tree, as well as provide insight into its structure and function through the use of numerous bioinformatics techniques. The information provided will hopefully assist in future research of this protein and related proteins.


Early literature review suggests that our protein is either RbsD or FucU, it is thought that both are of similar function. FucU may play a similar role as RbsD by binding L-fucose (Kim et al. 2003). It is tentatively suggested that these two proteins are involved in the binding, transport or possibly metabolism of sugar molecules in cells. Their involvement in any one of these processes is not yet clear or understood. It is thought RbsD and FucU play a role in the d-ribose and L-fucose transport respectively. D-ribose and L-fucose are forms of sugars and are used as energy sources. In the sequence analysis, RbsD shows no predicted transmembrane domain and exhibits sequence similarity to RbsD homologues in other organisms and to FucU, which is a component of the fucose operon (Kim et al 2001). Further research on these proteins has however identified possible biochemical functions. It seems that these two proteins are involved in the initial binding of the sugar molecules. Kim et al. (2003) demonstrated that the biochemical function of RbsD and FucU is to bind specific forms of D-ribose and fucose, respectively. This was concluded through the identification of conserved residues at the sugar binding sites.  Kim et al (2003) still has reservations about the exact function suggesting that the proteins play a role in facilitating the influx of the sugar substrates.





Latest revision as of 01:22, 16 June 2009

The sugars fucose and ribose both play an important role in the function of cells. Ribose is used in a range of cells for differing purposes, such as DNA, RNA synthesis and limited nutritional purposes. Fucose on the other hand plays an important role in cell receptors involved with cell to cell adhesion. Both of these sugars require transport systems to gain access into the cell. These transport systems used are called ATP-cassette binding (ABC) systems. These ATP-binding cassette (ABC)-type systems have been found to mediate the uptake of solutes such as amino acids, peptides, ions, vitamins, and sugars in a wide range of bacteria (Tuner et al. 1999).These ABC transport systems are found in all forms of life, both eukaryotes and prokaryotes. The structure of a typical prokaryote type ABC transporter consists of three types of components: two peripheral proteins that bind and hydrolyze ATP, two integral proteins each having six transmembrane segments and a periplasmic substrate binding protein (Igarashi et al 2004).

The FucU/RbsD superfamily of proteins are involved with the transport of fucose and ribose into the cell. These proteins are thought to be involved with the anomeric conversion of these two sugars . RbsD proteins convert beta-purine ribose into its furine counterpart (see figure 1) which is needed for the next step in metabolism. FucU proteins on the other hand catalyze the change of alpha-purine fucose into the beta form (see figure 2). The beta form is needed for use in the salvage pathway to form a number of important receptors and secretions (Kim et al. 2003).

Sugar.jpg

Figure 1.This shows the difference between the 5 ring franose and the six ring pruanose form of ribose. (Kim et al. 2003)


Fuc.jpg

Figure 2.This shows the difference between the alpha and beta form of fucose. (Ryu et al. 2007)


The 2ob5A protein (Hypothetical protein LOC282969 isoform 1) is found to be a member of the FucU/RbsD superfamily. The aim of this report is to provide information covering the evolutionary history of the protein through the construction of a phylogenic tree, as well as provide insight into its structure and function through the use of numerous bioinformatics techniques. The information provided will hopefully assist in future research of this protein and related proteins.



Abstract | Introduction | Method | Results | Discussion | Conclusion | References


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