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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ohnuma T,Umemoto N,Kondo K,Numata T,Fukamizo Tdoi
10.1016/j.febslet.2013.07.008subject
Has Abstractpub_date
2013-08-19 00:00:00pages
2691-7issue
16eissn
0014-5793issn
1873-3468pii
S0014-5793(13)00522-Xjournal_volume
587pub_type
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