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2.A.23.1.5
Archaeal aspartate transporter, Gltph (GltPh) (3-D structure known; 3V8F and 3V8G) (Boudker et al., 2007; Yernool et al., 2004). Cotransports aspartate with 2 Na+ (Ryan et al., 2009) or 3 Na+ (Groeneveld and Slotboom, 2010) or 1Na+ plus 1 H+ plus 1 K+ (Machtens et al. 2015). Reyes et al. (2009) have solved the structure of the inward facing state by cysteine crosslinking. The loop between TMSs 3 and 4 plays an essential role in transport (Compton et al., 2010). Gltph shows opposite movement of the external gate upon binding cotransported sodium compared with substrate (Focke et al., 2011).  The transport pathway and the conformational changes involved have been suggested based on modeling studies (Stolzenberg et al. 2012).  Individual transport domains may alternate between periods of quiescence and periods of rapid transitions.  The switch to the dynamic mode may be due to separation of the transport domain from the trimeric scaffold which precedes domain movements across the bilayer (Akyuz et al. 2013). This spontaneous dislodging of the substrate-loaded transport domain is approximately 100-fold slower than subsequent transmembrane movements and may be rate determining in the transport cycle.  Interactions between the transporter and specific lipids in artificial membranes have revealed effects on activity, and mechanisms have been proposed (McIlwain et al. 2015).  The system can also function as an anion channel (Machtens et al. 2015).

Accession Number:O59010
Protein Name:Proton glutamate symport protein
Length:425
Molecular Weight:44807.00
Species:Pyrococcus horikoshii [53953]
Number of TMSs:9
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate aspartate, glutamate, anions (channel function)

Cross database links:

HEGENOM: HBG739804
RefSeq: NP_143181.1   
Entrez Gene ID: 1443616   
Pfam: PF00375   
BioCyc: PHOR70601:PH1295-MONOMER   
KEGG: pho:PH1295   

Gene Ontology

GO:0016020 C:membrane
GO:0017153 F:sodium:dicarboxylate symporter activity
GO:0006835 P:dicarboxylic acid transport

References (2)

[1] “Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.”  Kawarabayasi Y.et.al.   9679194
[2] “Structure of a glutamate transporter homologue from Pyrococcus horikoshii.”  Yernool D.et.al.   15483603
Structure:
1XFH   2NWL   2NWW   2NWX   3KBC   3V8F   3V8G   4IZM   4OYE   4OYF   [...more]

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MGLYRKYIEY PVLQKILIGL ILGAIVGLIL GHYGYADAVK TYVKPFGDLF VRLLKMLVMP 
61:	IVFASLVVGA ASISPARLGR VGVKIVVYYL LTSAFAVTLG IIMARLFNPG AGIHLAVGGQ 
121:	QFQPKQAPPL VKILLDIVPT NPFGALANGQ VLPTIFFAII LGIAITYLMN SENEKVRKSA 
181:	ETLLDAINGL AEAMYKIVNG VMQYAPIGVF ALIAYVMAEQ GVKVVGELAK VTAAVYVGLT 
241:	LQILLVYFVL LKIYGIDPIS FIKKAKDAML TAFVTRSSSG TLPVTMRVAK EMGISEGIYS 
301:	FTLPLGATIN MDGTALYQGV CTFFIANALG SHLTVGQQLT IVLTAVLASI GTAGVPGAGA 
361:	IMLAMVLESV GLPLTDPNVA AAYAMILGID AILDMGRTMV NVTGDLTGTA IVAKTEGELE 
421:	KGVIA