Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.6.2.10 extracted from

  • Lemieux, M.J.; Huang, Y.; Wang, D.N.
    Crystal structure and mechanism of GlpT, the glycerol-3-phosphate transporter from E. coli (2005), J. Electron Microsc. (Tokyo), 54, i43-i46.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
into vector pBAD-MycHis-A and expressed in LMG194 cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
by vapor diffusion, to 3.3 A resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information GlpT appears to operate via a single binding-site, alternating-acess mechanism Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
inner membrane with periplasmic and cytoplasmic end Escherichia coli
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by Ni-NTA affinity column and size-exclusion chromatography Escherichia coli

Synonyms

Synonyms Comment Organism
GlpT
-
Escherichia coli
glycerol-3-phosphate transporter
-
Escherichia coli