|Entry||Database: PDB / ID: 2fz0|
|Title||Identification of yeast R-SNARE Nyv1p as a novel longin domain protein|
|Components||v-SNARE component of the vacuolar SNARE complex involved in vesicle fusion; inhibits ATP-dependent Ca(2+) transport activity of Pmc1p in the vacuolar membrane; Nyv1pSNARE (protein)|
|Keywords||MEMBRANE PROTEIN / SNARE protein / Longin domain|
|Function / homology|
Function and homology information
trans-Golgi Network Vesicle Budding / vacuole fusion, non-autophagic / SNARE complex / SNAP receptor activity / vesicle fusion / fungal-type vacuole membrane / vesicle-mediated transport / integral component of membrane
Similarity search - Function
Vacuolar R-SNARE Nyv1, longin domain / Vacuolar R-SNARE Nyv1, longin domain / Vacuolar R-SNARE Nyv1, longin domain superfamily / Vacuolar R-SNARE Nyv1, longin domain / Synaptobrevin / Synaptobrevin / v-SNARE, coiled-coil homology domain / v-SNARE coiled-coil homology domain profile. / Beta-Lactamase / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Vacuolar v-SNARE NYV1
Similarity search - Component
|Biological species||Saccharomyces cerevisiae (baker's yeast)|
|Method||SOLUTION NMR / simulated annealing|
|Authors||Wen, W. / Zhang, M.|
|Citation||Journal: Mol.Cell.Biol. / Year: 2006|
Title: Identification of the Yeast R-SNARE Nyv1p as a Novel Longin Domain-containing Protein
Authors: Wen, W. / Chen, L. / Wu, H. / Sun, X. / Zhang, M. / Banfield, D.K.
|Structure viewer||Molecule: |
Downloads & links
A: v-SNARE component of the vacuolar SNARE complex involved in vesicle fusion; inhibits ATP-dependent Ca(2+) transport activity of Pmc1p in the vacuolar membrane; Nyv1p
|#1: Protein|| |
Mass: 17014.383 Da / Num. of mol.: 1 / Fragment: longin domain, Residues 1-149
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (baker's yeast)
Plasmid: pETH / Production host: Escherichia coli (E. coli) / References: UniProt: Q12255
|Experiment||Method: SOLUTION NMR|
|Sample conditions||pH: 7.0 / Pressure: ambient / Temperature: 308 K|
|NMR software||Name: CNS / Version: 1.1 / Classification: refinement|
|Refinement||Method: simulated annealing / Software ordinal: 1|
|NMR representative||Selection criteria: lowest energy|
|NMR ensemble||Conformer selection criteria: structures with the lowest energy|
Conformers calculated total number: 200 / Conformers submitted total number: 20
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