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Crystal Structure Of Gh13 Alpha-Glucosidase Gsj From One Of The Deepest Sea Bacteria

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS(2008)

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摘要
The crystal structure of the GH13 alpha-glucosidase (GSJ) front deep-sea bacterium Geobacillus sp. strain HTA-462 A was determined to a 2.0 angstrom resolution. Comparisons of the GSJ structure with that of other GH13 enzymes with different catalytic activities revealed that the catalytic cleft of GSJ was widely opened when compared with the homologues. The wide opening of the catalytic cleft originated from conformational changes of active site residues and disorder of the regions close to the catalytic center. This structural feature of GSJ would explain the ability of this enzyme to accept a wide variety of nonsugar molecules as acceptors in the transglycosylation reaction.
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关键词
glucoside hydrolase, glycoconjugate, extremophile, protein evolution, structural bioinformatics
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