1xnf: Difference between revisions

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[[Image:1xnf.jpg|left|200px]]
{{Seed}}
[[Image:1xnf.png|left|200px]]


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{{STRUCTURE_1xnf|  PDB=1xnf  |  SCENE=  }}  
{{STRUCTURE_1xnf|  PDB=1xnf  |  SCENE=  }}  


'''Crystal structure of E.coli TPR-protein NlpI'''
===Crystal structure of E.coli TPR-protein NlpI===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15634341}}


==About this Structure==
==About this Structure==
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[[Category: Tetratricopeptide]]
[[Category: Tetratricopeptide]]
[[Category: Tpr]]
[[Category: Tpr]]
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Revision as of 10:21, 29 July 2008

File:1xnf.png

Template:STRUCTURE 1xnf

Crystal structure of E.coli TPR-protein NlpI

Template:ABSTRACT PUBMED 15634341

About this Structure

1XNF is a Single protein structure of sequence from Escherichia coli. 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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