Expression, purification, crystallization and preliminary X-ray analysis of the EIICGlc domain of the Escherichia coli glucose transporter

The glucose‐import system of Escherichia coli consists of a hydrophilic EIIAGlc subunit and a transmembrane EIICBGlc subunit. EIICBGlc (UniProt P69786) contains two domains: the transmembrane EIICGlc domain (40.6 kDa) and the cytoplasmic EIIBGlc domain (8.0 kDa), which are fused by a linker that is...

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Veröffentlicht in:	Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-06, Vol.66 (6), p.684-688
Hauptverfasser:	Zurbriggen, Andreas, Schneider, Philipp, Bähler, Priska, Baumann, Ulrich, Erni, Bernhard
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Crystallization Crystallization Communications Crystallography, X-Ray Escherichia coli Escherichia coli - chemistry Gene Expression Glucose Transport Proteins, Facilitative - chemistry Glucose Transport Proteins, Facilitative - genetics Glucose Transport Proteins, Facilitative - isolation & purification glucose transporters Molecular Sequence Data phosphotransferase systems Protein Structure, Tertiary
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Beschreibung
Zusammenfassung:	The glucose‐import system of Escherichia coli consists of a hydrophilic EIIAGlc subunit and a transmembrane EIICBGlc subunit. EIICBGlc (UniProt P69786) contains two domains: the transmembrane EIICGlc domain (40.6 kDa) and the cytoplasmic EIIBGlc domain (8.0 kDa), which are fused by a linker that is strongly conserved among its orthologues. The EIICBGlc subunit can be split within this motif by trypsin. Here, the crystallization of the tryptic EIICGlc domain is described. A complete data set was collected to 4.5 Å resolution at 100 K.
ISSN:	1744-3091 1744-3091
DOI:	10.1107/S1744309110013102