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Title 

Structural insights into conserved L-arabinose metabolic enzymes reveal the substrate binding site of a thermophilic L-arabinose isomerase

Authors 

Y J LeeS J LeeS B KimSang Jun LeeS H LeeD W Lee

Publisher 

Elsevier

Issue Date 

2014

Citation 

FEBS Letters, vol. 588, no. 6, pp. 1064-1070

Keywords 

l-Arabinose isomerasePredictionStructural genomicsSubstrate binding siteThermophilic

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 stearothermophilus l-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.

ISSN 

0014-5793

Link 

http://dx.doi.org/10.1016/j.febslet.2014.02.023

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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