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TitleStructural insights into the intrinsic self-assembly of Par-3 N-terminal domain.
Journal, issue, pagesStructure, Vol. 21, Issue 6, Page 997-991006, Year 2013
Publish dateJun 4, 2013
AuthorsYan Zhang / Wenjuan Wang / Jia Chen / Kai Zhang / Feng Gao / Bingquan Gao / Shuai Zhang / Mingdong Dong / Flemming Besenbacher / Weimin Gong / Mingjie Zhang / Fei Sun / Wei Feng /
PubMed AbstractPar-3, the central organizer of the Par-3/Par-6/atypical protein kinase C complex, is a multimodular scaffold protein that is essential for cell polarity establishment and maintenance. The N-terminal ...Par-3, the central organizer of the Par-3/Par-6/atypical protein kinase C complex, is a multimodular scaffold protein that is essential for cell polarity establishment and maintenance. The N-terminal domain (NTD) of Par-3 is capable of self-association to form filament-like structures, although the underlying mechanism is poorly understood. Here, we determined the crystal structure of Par-3 NTD and solved the filament structure by cryoelectron microscopy. We found that an intrinsic "front-to-back" interaction mode is important for Par-3 NTD self-association and that both the lateral and longitudinal packing within the filament are mediated by electrostatic interactions. Disruptions of the lateral or longitudinal packing significantly impaired Par-3 NTD self-association and thereby impacted the Par-3-mediated epithelial polarization. We finally demonstrated that a Par-3 NTD-like domain from histidine ammonia-lyase also harbors a similar self-association capacity. This work unequivocally provides the structural basis for Par-3 NTD self-association and characterizes one type of protein domain that can self-assemble via electrostatic interactions.
External linksStructure / PubMed:23643951
MethodsEM (helical sym.) / X-ray diffraction
Resolution2.9 - 6.1 Å
Structure data

2237

3zee

EMDB-2237: Electron cyro-microscopy helical reconstruction of Par-3 N-terminal domain
PDB-3zee: Electron cyro-microscopy helical reconstruction of Par-3 N terminal domain
Method: EM (helical sym.) / Resolution: 6.1 Å

PDB-4i6p:
Crystal structure of Par3-NTD domain
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsCELL CYCLE / SIGNALING PROTEIN / PB1 like motif / DUF3534 / Cell polarity protein

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