7RCP: GltPh mutant

GltPh mutant (S279E/D405N) in complex with aspartate and sodium ions. Determined by electron microscopy at 2.2 Å resolution. Released 20 Apr 2022.

Method: Electron microscopy
Resolution: 2.2 Å
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Chains: 3
Atoms: 9,339
Mol. weight: 132.32 kDa
Ligands: ASP
Released: 20 Apr 2022

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

Secondary structure: helices and β-sheets

7RCP contains 75 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: 25 helices, 0 β-strands

Element	Residues	Length
α-helix	3-9	7
α-helix	12-32	21
α-helix	36-38	3
α-helix	39-43	5
α-helix	44-56	13
α-helix	58-72	15
α-helix	75-106	32
α-helix	123-125	3
α-helix	127-129	3
α-helix	130-135	6
α-helix	142-147	6
α-helix	151-169	19
α-helix	174-220	47
α-helix	221-223	3
α-helix	227-242	16
α-helix	243-248	6
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	335-351	17
α-helix	358-369	12
α-helix	377-388	12
α-helix	390-415	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glutamate transporter homolog	A, B, C	protein	415	Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)	O59010 (AlphaFold model)

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

>7RCP_1 Glutamate transporter homolog (chains A, B, C)
GLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMPI
VFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQ
FQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSAE
TLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLTL
QILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSEGTLPVTMRVAKEMGISEGIYSF
TLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGAI
MLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGNLTGTAIVAKTE

Ligands and cofactors

ID	Name	Formula	Copies
ASP	Aspartic acid	C4 H7 N O4	3

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

Primary citation

The archaeal glutamate transporter homologue GltPh shows heterogeneous substrate binding. Reddy, K.D., Ciftci, D., Scopelliti, A.J. et al. J Gen Physiol (2022) 154. DOI 10.1085/jgp.202213131 · PubMed

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

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
9BH1 3.1 Å, Apo GltPh, intermediate outward-facing state

Browse structure collections

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