Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli
By Yafei Huang, M. J. Lemieux, Jinmei Song, M. Auer, Da-Neng Wang. Science, 2003
1,041 citations recorded by the source corpus.
Subfields: Genetics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/5e050379a8786645de028d0c56507498d98ecb2f
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In Genetics
- Xian-Zhi Li
- Debora Marks
- Christopher Sander
- Bernard Henrissat
- Curtis Huttenhower
- Can V. Tran
- Ravi D. Barabote
- Milton H. Saier Jr.
In Molecular Biology
- Curtis Huttenhower
- Debora Marks
- Christopher Sander
- Nicola Segata
- Burkhard Rost
- Lucy J. Colwell
- Thomas A. Hopf
- David T. Jones
Citations in the corpus
- Metabolic Reconstruction for Metagenomic Data and Its Application to the Human Microbiome (2012, background): “Two of these extended the categories listed above; the remainder comprised sn-Glycerol 3-phosphate transport (M00198, a membrane lipid precursor [32]), the mannose and trehalose phosphotransferase systems (M00270 and M00276), spermidine/putrescine transport (M00299), early terpenoid biosynthesis…”
- Efflux-Mediated Drug Resistance in Bacteria: an Update (2009, background): “[71] To date, crystal structures are available for several MFS transporters such as the lactose/H+ permease LacY,[72] the glycerol-3-phosphate transporter GlpT[73] and the multidrug transporter EmrD,[60] which are all from E. coli.”
- Mechanisms of neurotransmitter release by amphetamines: a review. (2005, background): “…model, in which tilting of transporter domains would close a ''cavity'' on the cytoplasmic side (the inward-facing conformation) to thereby open a new ''cavity'' on the extracellular (or for bacteria, periplasmic) side (the outward-facing conformation ) (Huang et al., 2003; Locher et al., 2003).”
- Protein structure prediction from sequence variation (2012, background): “An interesting example of covariation analysis of conformational changes is the derivation from computed evolutionary constraints of the alternative three-dimensional conformations in the large ‘major facilitator’ super-family of transmembrane proteins 22,52,53 .”
- The SLC2 (GLUT) Family of Membrane Transporters (2013, neutral): “…members of the MFS, have thus far proven recalcitrant to crystallization, but the crystal structures of 4 bacterial members of the MFS have been determined to at least moderate resolution by x-ray diffraction analysis (Abramson et al., 2003; Dang et al., 2010; Huang et al., 2003; Yin et al., 2006).”
- A glimpse of structural biology through X-ray crystallography. (2014, background): “, 2003) and the glycerol-3-phosphate transporter GlpT (Huang et al., 2003) (Figure 5A).”
- TCDB: the Transporter Classification Database for membrane transport protein analyses and information (2005, background): “The recent high-resolution structural elucidation of many transporters [such as BtuB (1,2), AcrB (3), LacY (4), GlpT (5), EmrE (6) and MsbA (7,8)] has enabled investigation into the molecular dynamics of fundamental transport processes.”
- Membrane-protein topology (2006, background): “Small-molecule transporters such as lactose permease and the glycerol-3-phosphate transporter are also thought to undergo extensive repacking of their transmembrane helices during substrate transpor”
- Functional biology of plant phosphate uptake at root and mycorrhiza interfaces. (2007, background): “The three-dimensional structures of oxalate (OxlT), lactose (LacY) and glycerol-3-phosphate/inorganic phosphate (GlpT) transporters from Oxalobacter formigens and Escherichia coli, respectively, have been elucidated; these demonstrate the presence of 12 transmembrane domains, substantiating the stru”
- 3D structures of membrane proteins from genomic sequencing (2012, positive): “…GlpT, residues with high total coupling scores line the substrate-binding sites and affect signaling or transport; for instance, W109, D113, and Y141 in Adrb2; K296, W265, and H211 in Opsd; and Y393, H165, and K90 in GlpT (Huang et al., 2003; Law et al., 2008; Valiquette et al., 1995) (Figure 6A).”