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Structural insights into conserved l ‐arabinose metabolic enzymes reveal the substrate binding site of a thermophilic l ‐arabinose isomerase
Author(s) -
Lee Yong-Jik,
Lee Sang-Jae,
Kim Seong-Bo,
Lee Sang Jun,
Lee Sung Haeng,
Lee Dong-Woo
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.02.023
Subject(s) - biochemistry , isomerase , structural similarity , thermophile , conserved sequence , enzyme , operon , geobacillus stearothermophilus , substrate (aquarium) , binding site , biology , chemistry , protein structure , peptide sequence , gene , mutant , ecology
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.