6X16: Glutamate transporter homologue GltPh

Inward-facing state of the glutamate transporter homologue GltPh in complex with TBOA. Determined by electron microscopy at 3.39 Å resolution. Released 18 Nov 2020.

Method: Electron microscopy
Resolution: 3.39 Å
Organism: Pyrococcus horikoshii
Chains: 3
Atoms: 9,438
Mol. weight: 136.8 kDa
Ligands: TB1, 6OU
Released: 18 Nov 2020

Explore 6X16 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6X16 contains 72 α-helices and 0 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A, B and C: 24 helices, 0 β-strands

Element	Residues	Length
α-helix	3-9	7
α-helix	12-32	21
α-helix	36-56	21
α-helix	58-73	16
α-helix	80-106	27
α-helix	123-129	7
α-helix	130-136	7
α-helix	142-147	6
α-helix	151-168	18
α-helix	175-219	45
α-helix	223-241	19
α-helix	242-248	7
α-helix	249-253	5
α-helix	258-264	7
α-helix	266-274	9
α-helix	282-290	9
α-helix	296-299	4
α-helix	302-309	8
α-helix	313-327	15
α-helix	333-334	2
α-helix	338-346	9
α-helix	359-370	12
α-helix	379-387	9
α-helix	391-413	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glutamate transporter homologue GltPh	A, B, C	protein	422	Pyrococcus horikoshii	O59010 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>6X16_1 Glutamate transporter homologue GltPh (chains A, B, C)
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLCMLVMP
IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ
QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA
ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS
FTLPLGATINMDGTALYQGVATFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA
IMLCMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV
PR

Ligands and cofactors

ID	Name	Formula	Copies
TB1	(3S)-3-(benzyloxy)-L-aspartic acid	C11 H13 N O5	3
6OU	[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-y…	C39 H76 N O8 P	3

Primary citation

Large domain movements through the lipid bilayer mediate substrate release and inhibition of glutamate transporters. Wang, X., Boudker, O. Elife (2020) 9. DOI 10.7554/eLife.58417 · PubMed

Other PDB entries of the same protein (UniProt O59010 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7RCP 2.2 Å, GltPh mutant (S279E/D405N) in complex with aspartate and sodium ions
7AHK 2.5 Å, Crystal structure of the outward-facing state of the substrate-free Na+-only bound…
7UG0 2.55 Å, TBOA-bound GltPh RSMR mutant in IFS state
9BH2 2.7 Å, Apo GltPh, outward-facing state
7UGJ 2.81 Å, TBOA-bound GltPh RSMR mutant in OFS state
7UGV 2.94 Å, Asp-bound GltPh RSMR mutant in IFS-A2 state
7UGD 2.95 Å, Asp-bound GltPh RSMR mutant in IFS-A1 state
2NWL 2.96 Å, Crystal structure of GltPh in complex with L-Asp
7UGX 2.96 Å, Asp-bound GltPh RSMR mutant in IFS-B1 state
7UH3 2.99 Å, Asp-bound GltPh RSMR mutant in iOFS state
6X15 3.05 Å, Inward-facing state of the glutamate transporter homologue GltPh in complex with…
6UWF 3.08 Å, GltPh in complex with L-aspartate and sodium ions in outward-facing state

Browse structure collections

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