TY - JOUR
T1 - Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain
AU - Crennell, Susan
AU - Garman, Elspeth
AU - Laver, Graeme
AU - Vimr, Eric
AU - Taylor, Garry
PY - 1994/6
Y1 - 1994/6
N2 - Background Vibrio cholerae neuraminidase is part of a mucinase complex which may function in pathogenesis by degrading the mucin layer of the gastrointestinal tract. The neuraminidase, which has been the target of extensive inhibitor studies, plays a subtle role in the pathology of the bacterium, by processing higher order gangliosides to G M1, the receptor for cholera toxin. Results We report here the X-ray crystal structure of V. cholerae neuraminidase at 2.3 å resolution. The 83 kDa enzyme folds into three distinct domains. The central catalytic domain has the canonical neuraminidase β -propeller fold, and is flanked by two domains which possess identical legume lectin-like topologies but without the usual metal-binding loops. The active site has many features in common with other viral and bacterial neuraminidases but, uniquely, has an essential Ca 2+ ion which plays a crucial structural role. Conclusions The environment of the small intestine requires V. cholerae to secrete several adhesins, and it is known that its neuraminidase can bind to cell surfaces, and remain active. The unexpected lectin-like domains possibly mediate this attachment. These bacterial lectin folds represent additional members of a growing lectin superfamily.
AB - Background Vibrio cholerae neuraminidase is part of a mucinase complex which may function in pathogenesis by degrading the mucin layer of the gastrointestinal tract. The neuraminidase, which has been the target of extensive inhibitor studies, plays a subtle role in the pathology of the bacterium, by processing higher order gangliosides to G M1, the receptor for cholera toxin. Results We report here the X-ray crystal structure of V. cholerae neuraminidase at 2.3 å resolution. The 83 kDa enzyme folds into three distinct domains. The central catalytic domain has the canonical neuraminidase β -propeller fold, and is flanked by two domains which possess identical legume lectin-like topologies but without the usual metal-binding loops. The active site has many features in common with other viral and bacterial neuraminidases but, uniquely, has an essential Ca 2+ ion which plays a crucial structural role. Conclusions The environment of the small intestine requires V. cholerae to secrete several adhesins, and it is known that its neuraminidase can bind to cell surfaces, and remain active. The unexpected lectin-like domains possibly mediate this attachment. These bacterial lectin folds represent additional members of a growing lectin superfamily.
KW - Vibrio cholerae structure
KW - lectin
KW - neuraminidase
KW - sialidase
KW - structure
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U2 - 10.1016/S0969-2126(00)00053-8
DO - 10.1016/S0969-2126(00)00053-8
M3 - Article
C2 - 7922030
AN - SCOPUS:0028773635
VL - 2
SP - 535
EP - 544
JO - Structure with Folding & design
JF - Structure with Folding & design
SN - 0969-2126
IS - 6
ER -