Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 18, 2013, Pages 7264-7269

  Śledź, Paweł ^a   Unverdorben, Pia ^a   Beck, Florian ^a   Pfeifer, Günter ^a   Schweitzer, Andreas ^a   Förster, Friedrich ^a   Baumeister, Wolfgang ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

AAA ATPase; Hybrid methods in structural biology; Ubiquitin proteasome pathway

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE GAMMA S; ENDOPEPTIDASE CLPX; NUCLEOTIDE; PROTEASOME; PROTEASOME 26S; UNCLASSIFIED DRUG;

ARTICLE; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SACCHAROMYCES CEREVISIAE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BINDING SITES; MODELS, MOLECULAR; NUCLEOTIDES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

EID: 84876909425     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1305782110     Document Type: Article

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