AI Article Synopsis
- The study focuses on a mutant form of GH19 chitinase from rye seeds, specifically the double mutant RSC-c, which has Glu67 and Trp72 replaced by glutamine and alanine, respectively.
- Crystallographic analysis showed that two chitin tetrasaccharide (GlcNAc)₄ molecules occupy the enzyme's substrate-binding cleft, with one molecule binding to specific subsites and the other to overlapping regions.
- The research provides the first complete map of enzyme subsites for GH19 chitinase and suggests that conformational changes in the enzyme are crucial for its catalytic function.
Article Abstract
Crystallographic analysis of a mutated form of "loopful" GH19 chitinase from rye seeds a double mutant RSC-c, in which Glu67 and Trp72 are mutated to glutamine and alanine, respectively, (RSC-c-E67Q/W72A) in complex with chitin tetrasaccharide (GlcNAc)₄ revealed that the entire substrate-binding cleft was completely occupied with the sugar residues of two (GlcNAc)₄ molecules. One (GlcNAc)₄ molecule bound to subsites -4 to -1, while the other bound to subsites +1 to +4. Comparisons of the main chain conformation between liganded RSC-c-E67Q/W72A and unliganded wild type RSC-c suggested domain motion essential for catalysis. This is the first report on the complete subsite mapping of GH19 chitinase.
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| http://dx.doi.org/10.1016/j.febslet.2013.07.008 | DOI Listing |
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