Functional and Structural Studies of a Multidomain Alginate Lyase from Persicobacter sp CCB-QB2

被引:41
作者
Sim, Pei-Fang [1 ]
Furusawa, Go [1 ]
Teh, Aik-Hong [1 ]
机构
[1] Univ Sains Malaysia, Ctr Chem Biol, 10 Persiaran Bukit Jambul, Bayan Lepas 11900, Penang, Malaysia
来源
SCIENTIFIC REPORTS | 2017年 / 7卷
关键词
CARBOHYDRATE-BINDING MODULES; SUBSTRATE RECOGNITION; SEQUENCE-ANALYSIS; URONIC-ACID; EXPRESSION; CLONING; GROWTH; GENE; OLIGOSACCHARIDES; SACCHARIFICATION;
D O I
10.1038/s41598-017-13288-1
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
AlyQ from Persicobacter sp. CCB-QB2 is an alginate lyase with three domains - a carbohydrate-binding domain modestly resembling family 16 carbohydrate-binding module (CBM16), a family 32 CBM (CBM32) domain, and an alginate lyase domain belonging to polysaccharide lyase family 7 (PL7). Although AlyQ can also act on polyguluronate (poly-G) and polymannuronate (poly-M), it is most active on alginate. Studies with truncated AlyQ showed that the CBM32 domain did not contribute to enhancing AlyQ's activity under the assayed conditions. Nevertheless, it could bind to cleaved but not intact alginate, indicating that the CBM32 domain recognises alginate termini. The crystal structure containing both CBM32 and catalytic domains show that they do not interact with one another. The CBM32 domain contains a conserved Arg that may bind to the carboxyl group of alginate. The catalytic domain, meanwhile, shares a conserved substrate-binding groove, and the presence of two negatively charged Asp residues may dictate substrate specificity especially at subsite + 1. As Persicobacter sp. CCB-QB2 was unable to utilise alginate, AlyQ may function to help the bacterium degrade cell walls more efficiently.
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页数:9
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