TY - JOUR
T1 - Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure
AU - Ohnuma, Takayuki
AU - Umemoto, Naoyuki
AU - Kondo, Kaori
AU - Numata, Tomoyuki
AU - Fukamizo, Tamo
N1 - Funding Information:
This work was supported by “Strategic Project to Support the Formation of Research Bases at Private Universities: Matching Fund Subsidy from MEXT (Ministry of Education, Culture, Sports, Science and Technology), 2011–2015 (S1101035).
PY - 2013/8/19
Y1 - 2013/8/19
N2 - 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.
AB - 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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U2 - 10.1016/j.febslet.2013.07.008
DO - 10.1016/j.febslet.2013.07.008
M3 - Article
C2 - 23871710
AN - SCOPUS:84881476127
SN - 0014-5793
VL - 587
SP - 2691
EP - 2697
JO - FEBS Letters
JF - FEBS Letters
IS - 16
ER -