1XNF

Crystal structure of E.coli TPR-protein NlpI

Summary for 1XNF

• Entry DOI: 10.2210/pdb1xnf/pdb
• Descriptor: Lipoprotein nlpI, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• Functional Keywords: nlpi, tpr, tetratricopeptide, lipoprotein, structural genomics, unknown function
• Biological source: Escherichia coli
• Cellular location: Cell membrane; Lipid-anchor: P39833
• Total number of polymer chains: 2
• Total formula weight: 63603.70

Authors

Wilson, C.G.,Kajander, T.,Regan, L. (deposition date: 2004-10-04, release date: 2004-11-16, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.98 Å)