The temperature activated HtrA protease from pathogen Chlamydia trachomatis acts as both a chaperone and protease at 37 °C

FEBS Letters

Volumn 581, Issue 18, 2007, Pages 3382-3386

  Huston, Wilhelmina M ^a   Swedberg, Joaquim E ^a   Harris, Jonathan M ^a   Walsh, Terence P ^a   Mathews, Sarah A ^a   Timms, Peter ^a  

^a QUEENSLAND UNIVERSITY OF TECHNOLOGY   (Australia)

Author keywords

Chaperone; Chlamydia; HtrA; Serine protease

Indexed keywords

CHAPERONE; INSULIN; PROTEINASE; RECOMBINANT PROTEIN; SERINE PROTEINASE; SERINE PROTEINASE OMI;

ARTICLE; CHLAMYDIA TRACHOMATIS; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; TEMPERATURE; TEMPERATURE SENSITIVITY;

AMINO ACID SEQUENCE; CASEINS; CHLAMYDIA TRACHOMATIS; CIRCULAR DICHROISM; ENZYME ACTIVATION; HEAT-SHOCK PROTEINS; INSULIN; LACTALBUMIN; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SERINE; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY; TEMPERATURE;

BACTERIA (MICROORGANISMS); CHLAMYDIA; CHLAMYDIA TRACHOMATIS;

EID: 34447272291     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.06.039     Document Type: Article

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