A conserved fold for fimbrial components revealed by the crystal structure of a putative fimbrial assembly protein (BT1062) fromBacteroides thetaiotaomicronat 2.2 Å resolution
Year: 2010
Type: article
Abstract: 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.
Authors: Qingping Xu, Polat Abdubek, Tamara Astakhova, Herbert L. Axelrod, Constantina Bakolitsa, Xiaohui Cai, Dennis Carlton, Connie Chen, Hsiu-Ju Chiu, Michelle Chiu, Thomas Clayton, Debanu Das, Marc C. Deller, Lian Duan, Kyle Ellrott, Carol L. Farr, Julie Feuerhelm, Joanna C. Grant, Anna Grzechnik, Gye Won Han, Lukasz Jaroszewski, Kevin K. Jin, Heath E. Klock, Mark W. Knuth, Piotr Kozbial, S. Sri Krishna, Abhinav Kumar, David Marciano, Daniel McMullan, Mitchell D. Miller, Andrew T. Morse, Edward Nigoghossian, Amanda Nopakun, Linda Okach, Christina Puckett, Ron Reyes, Natasha Sefcovic, Henry J. Tien, Christine B. Trame, Henry van den Bedem, Dana Weekes, Tiffany Wooten, Andrew Yeh, Jiadong Zhou, Keith O. Hodgson, John Wooley, Marc-Andre Elsliger, Ashley M. Deacon, Adam Godzik, Scott A. Lesley, Ian A. Wilson
Institutions: SLAC National Accelerator Laboratory, Joint Center for Structural Genomics, Stanford Synchrotron Radiation Lightsource, Genomics Institute of the Novartis Research Foundation, University of California San Diego, Sanford Burnham Prebys Medical Discovery Institute, Scripps Research Institute
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Award: G2391189260
OpenAlex ID: W2015639119