2.A.23.1.14 Sodium:glutamate cotransporter (symporter), Glt, of 430 aas and probably 9 TMSs in a 3 + 3 + 3 TMS arrangement. Several 3-d structures are known (Jensen et al. 2013). The binding and transport of L- and D-aspartate have been studied, revealing that both the L- and D-aspartate bound GltTk structures with only minor rearrangements in the structure of the binding site (Arkhipova et al. 2019). A conserved methionine residue plays a role in the ion symport process, apparently by influencing the specific kinetics in the binding reaction, which, while influential for the turnover rate, does not fundamentally explain the ion-coupling mechanism (Zhou et al. 2021). The 3-d structure is available (PDB # 6XWO). It has a covalent trimeric transporter structure with an interconnecting rigid scafford domain (trimerization domain) on the inside. This seems to be a unique structure for a transporter (Colucci et al. 2023). The structure of the P208R mutant is also known (Colucci et al. 2023).
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Accession Number: | Q5JID0 |
Protein Name: | Proton/glutamate symporter, SDF family |
Length: | 430 |
Molecular Weight: | 45546.00 |
Species: | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) [69014] |
Number of TMSs: | 9 |
Location1 / Topology2 / Orientation3: |
Membrane1 / Multi-pass membrane protein2 |
Substrate |
anion, sodium(1+), hydron, L-aspartate(1-), glutamate(2-) |
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1: MGKSLLRRYL DYPVLWKILW GLVLGAVFGL IAGHFGYAGA VKTYIKPFGD LFVRLLKMLV
61: MPIVLASLVV GAASISPARL GRVGVKIVVY YLATSAMAVF FGLIVGRLFN VGANVNLGSG
121: TGKAIEAQPP SLVQTLLNIV PTNPFASLAK GEVLPVIFFA IILGIAITYL MNRNEERVRK
181: SAETLLRVFD GLAEAMYLIV GGVMQYAPIG VFALIAYVMA EQGVRVVGPL AKVVGAVYTG
241: LFLQIVITYF ILLKVFGIDP IKFIRKAKDA MITAFVTRSS SGTLPVTMRV AEEEMGVDKG
301: IFSFTLPLGA TINMDGTALY QGVTVLFVAN AIGHPLTLGQ QLVVVLTAVL ASIGTAGVPG
361: AGAIMLAMVL QSVGLDLTPG SPVALAYAMI LGIDAILDMG RTMVNVTGDL AGTVIVAKTE
421: KELDESKWIS