3M3W

Crystal structure of mouse PACSIN3 BAR domain mutant

Summary for 3M3W

• Entry DOI: 10.2210/pdb3m3w/pdb
• Descriptor: Protein kinase C and casein kinase II substrate protein 3 (2 entities in total)
• Functional Keywords: mouse, pacsin3, bar domain, endocytosis
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 2
• Total formula weight: 74695.65

Authors

Meng, G.,Bai, X.Y. (deposition date: 2010-03-10, release date: 2011-03-16, Last modification date: 2024-03-20)

Primary citation

Bai, X.Y.,Meng, G.,Luo, M.,Zheng, X.F.
Rigidity of wedge loop in PACSIN 3 protein is a key factor in dictating diameters of tubules
J.Biol.Chem., 287:22387-22396, 2012

PubMed Abstract: BAR (Bin/amphiphysin/Rvs) domain-containing proteins participate in cellular membrane remodeling. The F-BAR proteins normally generate low curvature tubules. However, in the PACSIN subfamily, the F-BAR domain from PACSIN 1 and 2 can induce both high and low curvature tubules. We found that unlike PACSIN 1 and 2, PACSIN 3 could only induce low curvature tubules. To elucidate the key factors that dictate the tubule curvature, crystal structures of all three PACSIN F-BAR domains were determined. A novel type of lateral interaction mediated by a wedge loop is observed between the F-BAR neighboring dimers. Comparisons of the structures of PACSIN 3 with PACSIN 1 and 2 indicate that the wedge loop of PACSIN 3 is more rigid, which influences the lateral interactions between assembled dimers. We further identified the residues that affect the rigidity of the loop by mutagenesis and determined the structures of two PACSIN 3 wedge loop mutants. Our results suggest that the rigidity-mediated conformations of the wedge loop correlate well with the various crystal packing modes and membrane tubulations. Thus, the rigidity of the wedge loop is a key factor in dictating tubule diameters.

PubMed: 22573331
DOI: 10.1074/jbc.M112.358960

Experimental method

X-RAY DIFFRACTION (2.6 Å)