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Volumn 272, Issue 37, 1997, Pages 23239-23246
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Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding
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Author keywords
[No Author keywords available]
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Indexed keywords
ADENOSINE TRIPHOSPHATE;
BACTERIAL PROTEIN;
MEMBRANE PROTEIN;
ARTICLE;
BACTERIAL MEMBRANE;
ESCHERICHIA COLI;
MEMBRANE STRUCTURE;
MEMBRANE TRANSPORT;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN STRUCTURE;
ADENOSINE TRIPHOSPHATASES;
ADENOSINE TRIPHOSPHATE;
AMINO ACID SEQUENCE;
ATP-BINDING CASSETTE TRANSPORTERS;
BACTERIAL PROTEINS;
BIOLOGICAL TRANSPORT;
CARRIER PROTEINS;
CELL FRACTIONATION;
CELL MEMBRANE;
CYSTEINE;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
MEMBRANE PROTEINS;
MEMBRANE TRANSPORT PROTEINS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MONOSACCHARIDE TRANSPORT PROTEINS;
MUTAGENESIS, SITE-DIRECTED;
PEPTIDE FRAGMENTS;
PEPTIDE MAPPING;
PROTEIN CONFORMATION;
PROTEIN PRECURSORS;
SEQUENCE HOMOLOGY, AMINO ACID;
SPECIES SPECIFICITY;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
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EID: 0030752693
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.272.37.23239 Document Type: Article |
Times cited : (93)
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References (21)
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