4FMM

Dimeric Sec14 family homolog 3 from Saccharomyces cerevisiae presents some novel features of structure that lead to a surprising "dimer-monomer" state change induced by substrate binding

Descriptor	Phosphatidylinositol transfer protein PDR16, GLYCEROL, MAGNESIUM ION, ... (4 entities in total)
Functional Keywords	sec14 domain, phosphatidylinositol binding, signaling protein, lipid binding protein
Biological source	Saccharomyces cerevisiae (yeast)
Cellular location	Lipid droplet P53860
Total number of polymer chains	2
Total molecular weight	84878.22
Authors	Yuan, Y.,Zhao, W.,Wang, X.,Gao, Y.,Niu, L.,Teng, M. (deposition date: 2012-06-18, release date: 2013-02-27, Last modification date: 2013-06-19)
Primary citation	Yuan, Y.,Zhao, W.,Wang, X.,Gao, Y.,Niu, L.,Teng, M. Dimeric Sfh3 has structural changes in its binding pocket that are associated with a dimer-monomer state transformation induced by substrate binding. Acta Crystallogr.,Sect.D, 69:313-323, 2013 PubMed: 23519406 (PDB entries with the same primary citation) DOI: 10.1107/S0907444912046161 Import into Mendeley
Experimental method	X-RAY DIFFRACTION (2.34 Å)

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