The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assemblies

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

Volumn 108, Issue 26, 2011, Pages 10490-10495

  Wrase, Robert ^a   Scott, Hannah ^a   Hilgenfeld, Rolf ^a,b,c   Hansen, Guido ^a  

^a UNIVERSITY OF LÜBECK   (Germany)

^b DESY   (Germany)

^c SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

Author keywords

Molecular switch; Oligomerization; PDZ domain; Protein quality control; X ray crystallography

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; DEGP PROTEIN; DEGQ PROTEIN; PROTEINASE; SERINE PROTEINASE OMI; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL ANALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; CYTOPLASM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; LEGIONELLA; LEGIONELLA FALLONII; MUTAGENIC ACTIVITY; NONHUMAN; OPTICAL RESOLUTION; PRIORITY JOURNAL; PROKARYOTE; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN SECRETION; PROTEIN VARIANT; SEQUENCE HOMOLOGY;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; LEGIONELLA; MODELS, MOLECULAR; PEPTIDE HYDROLASES; PROTEIN CONFORMATION;

ESCHERICHIA COLI; LEGIONELLA; LEGIONELLA FALLONII; PROKARYOTA;

EID: 79960601819     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1101084108     Document Type: Article

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