Volume 66, Issue 10 pp. 1281-1286
Open Access

A 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

Qingping XuPolat AbdubekTamara AstakhovaHerbert L. AxelrodConstantina BakolitsaXiaohui CaiDennis CarltonConnie ChenHsiu-Ju ChiuMichelle ChiuThomas ClaytonDebanu DasMarc C. DellerLian DuanKyle EllrottCarol L. FarrJulie FeuerhelmJoanna C. GrantAnna GrzechnikGye Won HanLukasz JaroszewskiKevin K. JinHeath E. KlockMark W. KnuthPiotr KozbialS. Sri KrishnaAbhinav KumarDavid MarcianoDaniel McMullanMitchell D. MillerAndrew T. MorseEdward NigoghossianAmanda NopakunLinda OkachChristina PuckettRon ReyesNatasha SefcovicHenry J. TienChristine B. TrameHenry Van Den BedemDana WeekesTiffany WootenAndrew YehJiadong ZhouKeith O. HodgsonJohn WooleyMarc-Andre ElsligerAshley M. DeaconAdam GodzikScott A. LesleyIan A. Wilson
First published: 18 October 2010
Citations: 3
Ian A. Wilson, e-mail: [email protected]

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.

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