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Structure paper

TitleStructure and Activity of the N-Terminal Substrate Recognition Domains in Proteasomal Atpases.
Journal, issue, pagesMol. Cell, Vol. 34, Page 580-, Year 2009
Publish dateApr 15, 2009 (structure data deposition date)
AuthorsDjuranovic, S. / Hartmann, M.D. / Habeck, M. / Ursinus, A. / Zwickl, P. / Martin, J. / Lupas, A.N. / Zeth, K.
External linksMol. Cell / PubMed:19481487
MethodsX-ray diffraction
Resolution1.6 - 2.5 Å
Structure data

PDB-2wfw:
Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases - The Arc domain structure
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-2wg5:
Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2wg6:
Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4, P61A Mutant
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • rhodococcus erythropolis (bacteria)
  • saccharomyces cerevisiae (brewer's yeast)
  • archaeoglobus fulgidus (archaea)
KeywordsATP-BINDING PROTEIN / PROTEASOMAL ATPASES / PAN / ARC / AAA / ATP-BINDING / NUCLEOTIDE-BINDING / TRANSCRIPTION / HYDROLASE / TRANSCRIPTION HYDROLASE COMPLEX / SUBSTRATE RECOGNITION / COILED COIL / AAA PROTEIN / CHAPERONE ACTIVITY / ATPASE / OB FOLD / CYTOPLASM / PROTEASOME / ATP-BINDING AMINO-ACID BIOSYNTHESIS / TRANSCRIPTION REGULATION / NUCLEUS / DNA-BINDING / ACTIVATOR / PHOSPHOPROTEIN

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