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

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 Lett

journal_title

FEBS letters

authors

Ohnuma T,Umemoto N,Kondo K,Numata T,Fukamizo T

doi

10.1016/j.febslet.2013.07.008

subject

Has Abstract

pub_date

2013-08-19 00:00:00

pages

2691-7

issue

16

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(13)00522-X

journal_volume

587

pub_type

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