- PDB-4zny: Structure of the human TSG101-UEV Domain in complex with the PTAP... -
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Basic information
Entry
Database: PDB / ID: 4zny
Title
Structure of the human TSG101-UEV Domain in complex with the PTAP motif of the p19 gag protein of the Human T-cell Leukemia type I virus
Components
T-cell leukemia virus type I, partial gag gene; HTLV1 (human T-lymphotropic virus type I)
Tumor susceptibility gene 101 protein
Keywords
PROTEIN TRANSPORT / ESCRT-I COMPLEX SUBUNIT TSG101
Function / homology
Function and homology information
positive regulation of viral budding via host ESCRT complex / positive regulation of ubiquitin-dependent endocytosis / extracellular transport / ESCRT I complex / regulation of extracellular exosome assembly / negative regulation of epidermal growth factor-activated receptor activity / viral budding / regulation of MAP kinase activity / exosomal secretion / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway ...positive regulation of viral budding via host ESCRT complex / positive regulation of ubiquitin-dependent endocytosis / extracellular transport / ESCRT I complex / regulation of extracellular exosome assembly / negative regulation of epidermal growth factor-activated receptor activity / viral budding / regulation of MAP kinase activity / exosomal secretion / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / membrane fission / positive regulation of exosomal secretion / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / multivesicular body assembly / virion binding / Flemming body / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / endosome to lysosome transport / negative regulation of epidermal growth factor receptor signaling pathway / viral budding via host ESCRT complex / autophagosome maturation / viral release from host cell / keratinocyte differentiation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / viral process / multivesicular body / HCMV Late Events / ubiquitin binding / regulation of cell growth / macroautophagy / Late endosomal microautophagy / protein modification process / Budding and maturation of HIV virion / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / symbiont-mediated suppression of host gene expression / transcription corepressor activity / calcium-dependent protein binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / late endosome / late endosome membrane / early endosome membrane / viral nucleocapsid / DNA recombination / DNA-directed DNA polymerase / Hydrolases; Acting on ester bonds / aspartic-type endopeptidase activity / early endosome / DNA-directed DNA polymerase activity / regulation of cell cycle / endosome membrane / endosome / symbiont entry into host cell / negative regulation of cell population proliferation / cell division / centrosome / ubiquitin protein ligase binding / protein-containing complex binding / nucleolus / structural molecule activity / negative regulation of transcription by RNA polymerase II / protein homodimerization activity / DNA binding / extracellular exosome / zinc ion binding / plasma membrane / cytosol / cytoplasm Similarity search - Function
Monochromator: Si(111) channel-cut crystal monochromator and a pair of KB mirrors Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.97779 Å / Relative weight: 1
Reflection
Redundancy: 4.7 % / Number: 37420 / Rmerge(I) obs: 0.032 / D res high: 2.4 Å / D res low: 19.96 Å / Num. obs: 8020 / % possible obs: 99.8
Resolution: 2.4→19.957 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 2 / Phase error: 35.62 / Stereochemistry target values: ML Details: The statistics of the data collection are those of the non-anomalous data, while the structure was refined with the anomalous data.
Rfactor
Num. reflection
% reflection
Rfree
0.2431
750
5.23 %
Rwork
0.2299
13590
-
obs
0.2306
14340
96.59 %
Solvent computation
Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
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