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Structures of PspAG97A α-glucoside hydrolase reveal a novel mechanism for chloride induced activation.

Abstract：

:Here we report the first crystal structure of a secretory α-glucoside hydrolase isolated from Pseudoalteromonas sp. K8, PspAG97A, which belongs to glycoside hydrolase family 97 and exhibits halophilic property. PspAG97A lacks an acidic surface, that is considered essential for protein stability at high salinity. Interestingly, PspAG97A unusually contains a chloride ion coordinated by the guanidinium group of Arg171 and the main chain amide groups of Tyr172 and Glu173 at the active site. The structures of PspAG97A complexed with acarbose and panose demonstrate that residues Glu173, Arg171 and Asn170 for subsite +1 decide the substrate specificity of the enzyme for the α-1,6-glucosidic linkage. Structural alterations observed in the R171K variant and enzyme kinetic experiments focusing on chloride assisted activation suggest that the active site chloride serves to properly orient Glu173, Arg171 and Asn170 to facilitate substrate recognition. Furthermore, the chloride assists the binding of Glu173 to the conserved calcium ion and plays an essential role in properly positioning the base catalyst Glu456. In sum, our results provide valuable insight into the structural basis of protein halophilicity.

journal_name

J Struct Biol

journal_title

Journal of structural biology

authors

He C,Li J,Li W,Xue Y,Fang Z,Fang W,Zhang X,Wang X,Xiao Y

doi

10.1016/j.jsb.2016.09.009

subject

Has Abstract

pub_date

2016-12-01 00:00:00

pages

426-436

issue

3

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(16)30198-8

journal_volume

196

pub_type

杂志文章

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