The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter

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

Volumn 102, Issue 30, 2005, Pages 10482-10486

  Gohlke, Ulrich ^a,e   Pullan, Lee ^a,f   McDevitt, Christopher A ^b   Porcelli, Ida ^b   De Leeuw, Erik ^b   Palmer, Tracy ^c,d   Saibil, Helen R ^a   Berks, Ben C ^b  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^d JOHN INNES CENTRE   (United Kingdom)

^e PSF Biotech AG   (Germany)

^f UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

Author keywords

Conical tilt reconstruction; Electron microscopy; Tat protein transport; Three dimensional structure; Twin arginine signal peptide

Indexed keywords

ARGININE; CARRIER PROTEIN; PROTEIN TATA; PROTEIN TATBC; PROTEINASE; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL MEMBRANE; CHLOROPLAST; ELECTRON MICROSCOPY; MEMBRANE PERMEABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; THYLAKOID MEMBRANE;

ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; IMAGE PROCESSING, COMPUTER-ASSISTED; MEMBRANE TRANSPORT PROTEINS; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; PROTEIN CONFORMATION;

ESCHERICHIA COLI;

EID: 23044487649     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0503558102     Document Type: Article

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