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1IOU

SOLUTION STRUCTURE OF YKT6P (1-140)

Summary for 1IOU
Entry DOI10.2210/pdb1iou/pdb
Related1h8m
DescriptorYKT6P (1 entity in total)
Functional Keywordssnare, membrane protein
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationCell membrane; Lipid-anchor; Cytoplasmic side (Potential): P36015
Total number of polymer chains1
Total formula weight15854.74
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 citationTochio, 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: 11474112
DOI: 10.1126/science.1062950
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

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