1xnf
From Proteopedia
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Crystal structure of E.coli TPR-protein NlpI
Overview
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.
About this Structure
1XNF is a Single protein structure of sequence from Escherichia coli with TRS as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold., Wilson CG, Kajander T, Regan L, FEBS J. 2005 Jan;272(1):166-79. PMID:15634341
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