Structural insights into conserved l-arabinose metabolic enzymes reveal the substrate binding site of a thermophilic l-arabinose isomerase |
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Authors: | Yong-Jik Lee Sang-Jae Lee Seong-Bo Kim Sang Jun Lee Sung Haeng Lee Dong-Woo Lee |
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Affiliation: | 1. School of Applied Biosciences, Kyungpook National University, Daegu 702-701, South Korea;2. CJ Foods R&D, CJ Cheiljedang Corporation, Seoul, South Korea;3. Infection & Immunity Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, South Korea;4. Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju 501-759, South Korea |
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Abstract: | Structural genomics demonstrates that despite low levels of structural similarity of proteins comprising a metabolic pathway, their substrate binding regions are likely to be conserved. Herein based on the 3D-structures of the α/β-fold proteins involved in the ara operon, we attempted to predict the substrate binding residues of thermophilic Geobacillus stearothermophilusl-arabinose isomerase (GSAI) with no 3D-structure available. Comparison of the structures of l-arabinose catabolic enzymes revealed a conserved feature to form the substrate-binding modules, which can be extended to predict the substrate binding site of GSAI (i.e., D195, E261 and E333). Moreover, these data implicated that proteins in the l-arabinose metabolic pathway might retain their substrate binding niches as the modular structure through conserved molecular evolution even with totally different structural scaffolds. |
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Keywords: | Structural genomics Prediction Substrate binding site l-Arabinose isomerase Thermophilic |
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