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Crystal structure of the ADP-ribosylating component of BEC, the binary enterotoxin of Clostridium perfringens.

Abstract：

:Binary enterotoxin of Clostridium perfringens (BEC), consisting of the components BECa and BECb, was recently identified as a novel enterotoxin produced by C. perfringens that causes acute gastroenteritis in humans. Although the detailed mechanism of cell intoxication by BEC remains to be defined, BECa shows both NAD+-glycohydrolase and actin ADP-ribosyltransferase activities in the presence of NAD+. In this study, we determined the first crystal structure of BECa in its apo-state and in complex with NADH. The structure of BECa shows striking resemblance with other binary actin ADP-ribosylating toxins (ADPRTs), especially in terms of its overall protein fold and mechanisms of substrate recognition. We present a detailed picture of interactions between BECa and NADH, including bound water molecules located near the C1'-N glycosidic bond of NADH and the catalytically important ADP-ribosylating turn-turn (ARTT) loop. We observed that the conformational rearrangement of the ARTT loop, possibly triggered by a conformational change involving a conserved tyrosine residue coupled with substrate binding, plays a crucial role in catalysis by properly positioning a catalytic glutamate residue in the E-X-E motif of the ARTT loop in contact with the nucleophile. Our results for BECa provide insight into the common catalytic mechanism of the family of binary actin ADPRTs.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kawahara K,Yonogi S,Munetomo R,Oki H,Yoshida T,Kumeda Y,Matsuda S,Kodama T,Ohkubo T,Iida T,Nakamura S

doi

10.1016/j.bbrc.2016.10.042

subject

Has Abstract

pub_date

2016-11-11 00:00:00

pages

261-267

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(16)31717-X

journal_volume

480

pub_type

杂志文章

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