7AHK: Glutamate transporter homolog

Crystal structure of the outward-facing state of the substrate-free Na+-only bound glutamate transporter homolog GltPh. Determined by X-ray diffraction at 2.5 Å resolution. Released 18 Nov 2020.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Pyrococcus horikoshii
Chains: 1
Atoms: 3,250
Mol. weight: 49.56 kDa
Ligands: OLC, LFA, PO4, BOG
Released: 18 Nov 2020

Explore 7AHK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7AHK contains 25 α-helices and 0 β-strands across 1 chain. 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.

Chain A: 25 helices, 0 β-strands

Element	Residues	Length
α-helix	13-32	20
α-helix	36-38	3
α-helix	39-43	5
α-helix	44-55	12
α-helix	58-70	13
α-helix	75-107	33
α-helix	115-116	2
α-helix	124-129	6
α-helix	130-135	6
α-helix	142-147	6
α-helix	151-168	18
α-helix	174-201	28
α-helix	205-219	15
α-helix	221-223	3
α-helix	227-241	15
α-helix	242-248	7
α-helix	249-253	5
α-helix	258-275	18
α-helix	278-291	14
α-helix	296-309	14
α-helix	312-329	18
α-helix	335-350	16
α-helix	358-368	11
α-helix	377-387	11
α-helix	390-415	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glutamate transporter homolog	A	protein	425	Pyrococcus horikoshii	O59010 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7AHK_1 Glutamate transporter homolog (chains A)
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMP
IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ
QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA
ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS
FTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA
IMLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV
PRGSG

Ligands and cofactors

ID	Name	Formula	Copies
OLC	(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate	C21 H40 O4	2
LFA	Eicosane	C20 H42	12
PO4	Phosphate ion	O4 P	1
BOG	octyl beta-D-glucopyranoside	C14 H28 O6	1

Water and common crystallization additives (GOL, NA) are not listed.

Primary citation

Na + -dependent gate dynamics and electrostatic attraction ensure substrate coupling in glutamate transporters. Alleva, C., Kovalev, K., Astashkin, R. et al. Sci Adv (2020) 6. DOI 10.1126/sciadv.aba9854 · 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
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
9BH1 3.1 Å, Apo GltPh, intermediate outward-facing state

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