1XNF

Crystal structure of E.coli TPR-protein NlpI

1XNF の概要

• エントリーDOI: 10.2210/pdb1xnf/pdb
• 分子名称: Lipoprotein nlpI, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• 機能のキーワード: nlpi, tpr, tetratricopeptide, lipoprotein, structural genomics, unknown function
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell membrane; Lipid-anchor: P39833
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63603.70

構造登録者

Wilson, C.G.,Kajander, T.,Regan, L. (登録日: 2004-10-04, 公開日: 2004-11-16, 最終更新日: 2024-10-09)

主引用文献

Wilson, C.G.,Kajander, T.,Regan, L.
The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold.
FEBS J., 272:166-179, 2005

PubMed Abstract: There are several different families of repeat proteins. In each, a distinct structural motif is repeated in tandem to generate an elongated structure. The nonglobular, extended structures that result are particularly well suited to present a large surface area and to function as interaction domains. Many repeat proteins have been demonstrated experimentally to fold and function as independent domains. In tetratricopeptide (TPR) repeats, the repeat unit is a helix-turn-helix motif. The majority of TPR motifs occur as three to over 12 tandem repeats in different proteins. The majority of TPR structures in the Protein Data Bank are of isolated domains. Here we present the high-resolution structure of NlpI, the first structure of a complete TPR-containing protein. We show that in this instance the TPR motifs do not fold and function as an independent domain, but are fully integrated into the three-dimensional structure of a globular protein. The NlpI structure is also the first TPR structure from a prokaryote. It is of particular interest because it is a membrane-associated protein, and mutations in it alter septation and virulence.

PubMed: 15634341
DOI: 10.1111/j.1432-1033.2004.04397.x

実験手法

X-RAY DIFFRACTION (1.98 Å)