1IOU
SOLUTION STRUCTURE OF YKT6P (1-140)
Summary for 1IOU
Entry DOI | 10.2210/pdb1iou/pdb |
Related | 1h8m |
Descriptor | YKT6P (1 entity in total) |
Functional Keywords | snare, membrane protein |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Cellular location | Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P36015 |
Total number of polymer chains | 1 |
Total formula weight | 15854.74 |
Authors | Tochio, H.,Tsui, M.M.K.,Banfield, D.K.,Zhang, M. (deposition date: 2001-04-09, release date: 2003-05-06, Last modification date: 2023-12-27) |
Primary citation | Tochio, H.,Tsui, M.M.K.,Banfield, D.K.,Zhang, M. An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p SCIENCE, 293:698-702, 2001 Cited by PubMed Abstract: Ykt6p is a nonsyntaxin SNARE implicated in multiple intracellular membrane trafficking steps. Here we present the structure of the NH2-terminal domain of Ykt6p (Ykt6pN, residues 1 to 140). The structure of Ykt6pN differed entirely from that of syntaxin and resembled the overall fold of the actin regulatory protein, profilin. Like some syntaxins, Ykt6p adopted a folded back conformation in which Ykt6pN bound to its COOH-terminal core domain. The NH2-terminal domain plays an important biological role in the function of Ykt6p, which in vitro studies revealed to include influencing the kinetics and proper assembly of SNARE complexes. PubMed: 11474112DOI: 10.1126/science.1062950 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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