Gill HS (2007) Structural Insights into the Exchange Domain of Sec2p: Expression, Purification, Crystallization, and Preliminary X-Ray Diffraction Data Analysis. Protein Pept Lett 14(3):253-258
Abstract: Sec2p is an essential yeast gene and is part of the cell polarization process that leads to budding. The N-terminal domain of sec2p (Sec2pN)—the guanine-nucleotide exchange factor for sec4p—has been expressed in Escherichia coli, purified, and crystallized. Crystals belong to the space group P2(1) with unit cell dimensions 178.1 x 98.4 x 180.0 A, beta = 91.7( degrees ), and diffract synchrotron-generated X-rays to better than 3.6 A resolution. Pseudo-precession plots reveal a Laue symmetry of 2/m, corresponding to the aforementioned space group, and unusual weak diffraction in the approximately 5-7 A resolution range. The Matthews number calculations for a typical crystal density suggest a range of 28 to 64 molecules per asymmetric unit. Self-rotation and native Patterson calculations demonstrate a pure helical array of protein subunits. Based on the X-ray diffraction data analysis and amino-acid sequence alignments, the paper presents a hypothetical model of the exchange domain of sec2p as a pair of coiled-coil helices that binds to sec4p and facilitates nucleotide disassociation.
|Status: Published||Type: Journal Article||PubMed ID: 17346229|
Topics addressed in this paper
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|Protein Physical Properties|
|Protein Sequence Features|
|Protein/Nucleic Acid Structure|