|
ИСТИНА |
Войти в систему Регистрация |
ИПМех РАН |
||
Catalytic and Lectin Domains in Neuraminidase A from Streptococcus pneumoniae are Capable of an Intermolecular Assembly: Implications for Biofilm Formationстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 9 декабря 2020 г.
- Авторы: Sharapova Yana, Svedas Vytas, Suplatov Dmitry
- Журнал: FEBS Journal
- Год издания: 2020
- Издательство: Blackwell Publishing Inc.
- Местоположение издательства: United Kingdom
- Номер статьи: febs.15610
- DOI: 10.1111/febs.15610
- Аннотация: Neuraminidase A from Streptococcus pneumoniae (NanA) is a cell wall‐bound modular enzyme containing one lectin and one catalytic domain. Unlike homologous NanB and NanC expressed by the same bacterium, the two domains within one NanA molecule do not form a stable interaction and are spatially separated by a 16 amino acids long flexible linker. In this work, the ability of NanA to form intermolecular assemblies was characterized using the methods of molecular modeling and bioinformatic analysis based on crystallographic data and by bringing together previously published experimental data. It was concluded that two catalytic domains, as well as one catalytic and one lectin domain, originating from two cell wall‐bound NanA molecules, can interact through a previously uncharacterized interdomain interface to form complexes stabilized by a network of intermolecular hydrogen bonds and salt bridges. Supercomputer modeling strongly indicated that artocarpin, an earlier experimentally discovered inhibitor of the pneumococcal biofilm formation, is able to bind to a site located in the catalytic domain of one NanA entity and prevent its interaction with the lectin or catalytic domain of another NanA entity, thus directly precluding the generation of intermolecular assemblies. The revealed structural adaptation is discussed as one plausible mechanism of non‐catalytic participation of this potentially key pathogenicity enzyme in pneumococcal biofilm formation.
- Добавил в систему: Шарапова Яна Александровна