glutamate and aspartate transporter subunit; Provisional

Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic binding protein fold. This subfamily represents the periplasmic-binding protein component of ABC transporter specific for carboxylic amino acids, including GtlI from Escherichia coli. The aspartate-glutamate binding domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.

Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold. This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.

Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 periplasmic-bindig protein fold. This group includes periplasmic glutamine-binding domain GlnP from Bacillus subtilis and its related proteins. The GlnP domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.

Bacterial extracellular solute-binding proteins, family 3.

DEBP[Shigella flexneri],2VHA_B DEBP [Shigella flexneri]

Crystalstructure of Novel amino acid binding protein from Shigella flexneri [Shigella flexneri 2a str. 301],2IA4_B Crystal structure of Novel amino acid binding protein from Shigella flexneri [Shigella flexneri 2a str. 301]

CrystalStructure of Solute-binding Protein from Enterococcus faecium with Bound Glutamate [Enterococcus faecium DO],5EYF_B Crystal Structure of Solute-binding Protein from Enterococcus faecium with Bound Glutamate [Enterococcus faecium DO]

Structureof the Campylobacter jejuni antigen Peb1A, an aspartate and glutamate receptor with bound aspartate [Campylobacter jejuni],2V25_B Structure of the Campylobacter jejuni antigen Peb1A, an aspartate and glutamate receptor with bound aspartate [Campylobacter jejuni]

Crystalstructure of the P235GK mutant of ArgBP from T. maritima [Thermotoga maritima MSB8]

L-glutamate/L-aspartate-binding protein OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=PA1342 PE=1 SV=1

Glutamate/aspartate import solute-binding protein OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=gltI PE=3 SV=3

Glutamate/aspartate import solute-binding protein OS=Escherichia coli (strain K12) OX=83333 GN=gltI PE=1 SV=2

ABC transporter glutamine-binding protein GlnH OS=Bacillus subtilis (strain 168) OX=224308 GN=glnH PE=2 SV=1

Glutamine-binding protein OS=Geobacillus stearothermophilus OX=1422 GN=glnH PE=3 SV=1