Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure

Takayuki Ohnuma, Naoyuki Umemoto, Kaori Kondo, Tomoyuki Numata, Tamo Fukamizo

Research output: Contribution to journalArticle

20 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2691-2697
Number of pages7
JournalFEBS Letters
Volume587
Issue number16
DOIs
Publication statusPublished - Aug 19 2013
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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