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Structure paper

TitleStructural basis for proteasome formation controlled by an assembly chaperone nas2.
Journal, issue, pagesStructure, Vol. 22, Page 731-743, Year 2014
Publish dateAug 26, 2013 (structure data deposition date)
AuthorsSatoh, T. / Saeki, Y. / Hiromoto, T. / Wang, Y.H. / Uekusa, Y. / Yagi, H. / Yoshihara, H. / Yagi-Utsumi, M. / Mizushima, T. / Tanaka, K. / Kato, K.
External linksStructure / PubMed:24685148
MethodsX-ray diffraction
Resolution1.65 - 4 Å
Structure data

PDB-3whj:
Crystal structure of Nas2 N-terminal domain
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-3whk:
Crystal structure of PAN-Rpt5C chimera
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3whl:
Crystal structure of Nas2 N-terminal domain complexed with PAN-Rpt5C chimera
Method: X-RAY DIFFRACTION / Resolution: 4 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-CD:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • pyrococcus furiosus (archaea)
KeywordsCHAPERONE / Proteasome assembly chaperone / HYDROLASE / Four-helix bundle / Proteasome ATPase subunit / ATP Binding / HYDROLASE/CHAPERONE / HYDROLASE-CHAPERONE complex

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