Open AccessA conserved fold for fimbrial components revealed by the crystal structure of a putative fimbrial assembly protein (BT1062) from Bacteroides thetaiotaomicron at 2.2 Å resolution
Author(s) -
Xu Qingping,
Abdubek Polat,
Astakhova Tamara,
Axelrod Herbert L.,
Bakolitsa Constantina,
Cai Xiaohui,
Carlton Dennis,
Chen Connie,
Chiu HsiuJu,
Chiu Michelle,
Clayton Thomas,
Das Debanu,
Deller Marc C.,
Duan Lian,
Ellrott Kyle,
Farr Carol L.,
Feuerhelm Julie,
Grant Joanna C.,
Grzechnik Anna,
Han Gye Won,
Jaroszewski Lukasz,
Jin Kevin K.,
Klock Heath E.,
Knuth Mark W.,
Kozbial Piotr,
Krishna S. Sri,
Kumar Abhinav,
Marciano David,
McMullan Daniel,
Miller Mitchell D.,
Morse Andrew T.,
Nigoghossian Edward,
Nopakun Amanda,
Okach Linda,
Puckett Christina,
Reyes Ron,
Sefcovic Natasha,
Tien Henry J.,
Trame Christine B.,
Van Den Bedem Henry,
Weekes Dana,
Wooten Tiffany,
Yeh Andrew,
Zhou Jiadong,
Hodgson Keith O.,
Wooley John,
Elsliger MarcAndre,
Deacon Ashley M.,
Godzik Adam,
Lesley Scott A.,
Wilson Ian A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110006548
Subject(s) - bacteroides thetaiotaomicron , fimbria , porphyromonas gingivalis , bacteroides , bacteroidaceae , fold (higher order function) , biology , chemistry , microbiology and biotechnology , genetics , bacteria , escherichia coli , gene , mechanical engineering , engineering
BT1062 from Bacteroides thetaiotaomicron is a homolog of Mfa2 (PGN0288 or PG0179), which is a component of the minor fimbriae in Porphyromonas gingivalis . The crystal structure of BT1062 revealed a conserved fold that is widely adopted by fimbrial components.