The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding

FEBS Letters

Volumn 562, Issue 1-3, 2004, Pages 183-188

  Campanacci, Valérie ^a   Nurizzo, Didier ^b   Spinelli, Silvia ^a   Valencia, Christel ^a,c   Tegoni, Mariella ^a   Cambillau, Christian ^a  

^a AIX MARSEILLE UNIVERSITY   (France)

^b EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^c Institut Gilbert Laustriat   (France)

Author keywords

Blc; Lipid transport; Lipocalin; Remote SAD; Structural genomics; Xenon

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; FATTY ACID; LIPOCALIN; PHOSPHOLIPID; XENON;

ALPHA HELIX; ARTICLE; CELL MEMBRANE; CELL REGENERATION; CRYSTAL STRUCTURE; CRYSTALLIZATION; ESCHERICHIA COLI; GENOMICS; LIPID STORAGE; LIPID TRANSPORT; MOTH; OSMOLARITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; BACTERIAL OUTER MEMBRANE PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LIPOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHOLIPIDS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; LEPIDOPTERA;

EID: 1642373041     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(04)00199-1     Document Type: Article

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