A conserved fold for fimbrial components revealed by the crystal structure of a putative fimbrial assembly protein (BT1062) from Bacteroides thetaiotaomicron at 2.2 angstrom resolution

作者：Xu Qingping; Abdubek Polat; Astakhova Tamara; Axelrod Herbert L; Bakolitsa Constantina; Cai Xiaohui; Carlton Dennis; Chen Connie; Chiu Hsiu Ju; 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

来源：Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 2010, 66: 1281-1286.

DOI：10.1107/S1744309110006548

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.

• 出版日期2010-10
• 单位河北医科大学