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5JAE

LeuT in the outward-oriented, Na+-free return state, P21 form at pH 6.5

Summary for 5JAE
Entry DOI10.2210/pdb5jae/pdb
DescriptorTransporter, octyl beta-D-glucopyranoside (3 entities in total)
Functional Keywordsmembrane protein, neurotransmitter:sodium symporter family, amino acid transporter
Biological sourceAquifex aeolicus (strain VF5)
Total number of polymer chains2
Total formula weight119370.93
Authors
Malinauskaite, L.,Sahin, C.,Said, S.,Grouleff, J.,Shahsavar, A.,Bjerregaard, H.,Noer, P.,Severinsen, K.,Boesen, T.,Schiott, B.,Sinning, S.,Nissen, P. (deposition date: 2016-04-12, release date: 2016-06-01, Last modification date: 2024-01-10)
Primary citationMalinauskaite, L.,Said, S.,Sahin, C.,Grouleff, J.,Shahsavar, A.,Bjerregaard, H.,Noer, P.,Severinsen, K.,Boesen, T.,Schitt, B.,Sinning, S.,Nissen, P.
A conserved leucine occupies the empty substrate site of LeuT in the Na(+)-free return state.
Nat Commun, 7:11673-11673, 2016
Cited by
PubMed Abstract: Bacterial members of the neurotransmitter:sodium symporter (NSS) family perform Na(+)-dependent amino-acid uptake and extrude H(+) in return. Previous NSS structures represent intermediates of Na(+)/substrate binding or intracellular release, but not the inward-to-outward return transition. Here we report crystal structures of Aquifex aeolicus LeuT in an outward-oriented, Na(+)- and substrate-free state likely to be H(+)-occluded. We find a remarkable rotation of the conserved Leu25 into the empty substrate-binding pocket and rearrangements of the empty Na(+) sites. Mutational studies of the equivalent Leu99 in the human serotonin transporter show a critical role of this residue on the transport rate. Molecular dynamics simulations show that extracellular Na(+) is blocked unless Leu25 is rotated out of the substrate-binding pocket. We propose that Leu25 facilitates the inward-to-outward transition by compensating a Na(+)- and substrate-free state and acts as the gatekeeper for Na(+) binding that prevents leak in inward-outward return transitions.
PubMed: 27221344
DOI: 10.1038/ncomms11673
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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