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Crystal Structure of a Family GH19 Chitinase (W72A/E67Q mutant) from rye seeds in complex with two (GlcNAc)4 moleculesCrystal Structure of a Family GH19 Chitinase (W72A/E67Q mutant) from rye seeds in complex with two (GlcNAc)4 molecules
Structural highlights
FunctionCHIC_SECCE Defense against chitin containing fungal pathogens. Binds the hyphal tips of fungi and degrades nascent chitin.[1] [2] [3] Publication Abstract from PubMedCrystallographic 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. Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure.,Ohnuma T, Umemoto N, Kondo K, Numata T, Fukamizo T FEBS Lett. 2013 Aug 19;587(16):2691-7. doi: 10.1016/j.febslet.2013.07.008. Epub, 2013 Jul 18. PMID:23871710[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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