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| =='''Report'''== | | =='''Report'''== |
| | [[Hypothetical protein Abstract | Abstract ]]<BR> |
| | [[Hypothetical protein Introduction | Introduction]]<BR> |
| | [[Hypothetical protein Method| Method]]<BR> |
| | [[Hypothetical protein Results | Results]]<BR> |
| | [[Hypothetical protein Discussion | Discussion]]<BR> |
| | [[Hypothetical protein Conclusion | Conclusion ]]<BR> |
| | [[Hypothetical protein References | References ]]<BR> |
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| [[Abstract]]
| | =='''Presentation'''== |
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| [[Introduction]] | | [[2ob5 Function presentation]] |
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| [[Methods]]
| | =='''Main Focus Areas'''== |
| | | [[Structure of 2ob5 | Structure]] | [[Main Hypothetical Protein Function Page | Function]] | [[Main Hypothetical Protein Evolution Page | Evolution]] |
| [[Results]] | |
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| [[Discussion]]
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| [[Conclusion]] | |
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| [[References]] | |
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| '''Breif Introduction'''
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| 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.
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| '''REFERENCES'''
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| J Biol Chem, Vol. 274, Issue 20, 14006-14011, May 14, 1999
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| A Mutated PtsG, the Glucose Transporter, Allows Uptake of D-Ribose*
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| Hyangee Oh, Yongkyu Park, and Chankyu Park
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| Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli RbsD, a component of the ribose-transport system with unknown biochemical function
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| Crystal Structures of RbsD Leading to the Identification of Cytoplasmic Sugar-binding Proteins with a Novel Folding Architecture
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| Min-Sung Kim,a Hyangee Oh,b Chankyu Parkb and Byung-Ha Oha*
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| NMR Application Probes a Novel and Ubiquitous Family of Enzymes That Alter Monosaccharide Configuration*
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| Kyoung-Seok Ryu, Changhoon Kim, Insook Kim, Seokho Yoo, Byong-Seok Choi, and Chankyu Park
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| Ribose Utilization with an Excess of Mutarotase Causes Cell Death Due to Accumulation of Methylglyoxal
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| Insook Kim,1 Eunjung Kim,1 Seokho Yoo,1 Daesung Shin,1 Bumchan Min,2 Jeeyeon Song,1 and Chankyu Park1*
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| '''PDB'''
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| 3e7m
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| 3dsa
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| 1ogc-f
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