7DJ2

Crystal structure of the G26C/E290S mutant of LeuT

Summary for 7DJ2

• Entry DOI: 10.2210/pdb7dj2/pdb
• Related: 7DII 7DIX 7DJ1 7DJC
• Descriptor: Na(+):neurotransmitter symporter (Snf family), LEUCINE, SODIUM ION, ... (5 entities in total)
• Functional Keywords: neurotransmitter transporter, nss, slc6, transport protein
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 2
• Total formula weight: 115806.55

Authors

Fan, J.,Xiao, Y.,Sun, Z.,Zhou, X. (deposition date: 2020-11-19, release date: 2021-04-07, Last modification date: 2023-11-29)

Primary citation

Fan, J.,Xiao, Y.,Quick, M.,Yang, Y.,Sun, Z.,Javitch, J.A.,Zhou, X.
Crystal structures of LeuT reveal conformational dynamics in the outward-facing states.
J.Biol.Chem., 296:100609-100609, 2021

PubMed Abstract: The neurotransmitter:sodium symporter (NSS) homolog LeuT from Aquifex aeolicus has proven to be a valuable model for studying the transport mechanism of the NSS family. Crystal structures have captured LeuT in key conformations visited during the transport cycle, allowing for the construction of a nearly complete model of transport, with much of the conformational dynamics studied by computational simulations. Here, we report crystal structures of LeuT representing new intermediate conformations between the outward-facing open and occluded states. These structures, combined with binding and accessibility studies, reveal details of conformational dynamics that can follow substrate binding at the central substrate binding site (S1) of LeuT in outward-facing states, suggesting a potential competition for direction between the outward-open and outward-occluded states at this stage during substrate transport. Our structures further support an intimate interplay between the protonation state of Glu290 and binding of Na1 that may ultimately regulate the outward-open-to-occluded transition.

PubMed: 33811858
DOI: 10.1016/j.jbc.2021.100609

Experimental method

X-RAY DIFFRACTION (2.4 Å)