Document Detail


Structure and mechanism of a Na+-independent amino acid transporter.
MedLine Citation:
PMID:  19608859     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Amino acid, polyamine, and organocation (APC) transporters are secondary transporters that play essential roles in nutrient uptake, neurotransmitter recycling, ionic homeostasis, and regulation of cell volume. Here, we present the crystal structure of apo-ApcT, a proton-coupled broad-specificity amino acid transporter, at 2.35 angstrom resolution. The structure contains 12 transmembrane helices, with the first 10 consisting of an inverted structural repeat of 5 transmembrane helices like the leucine transporter LeuT. The ApcT structure reveals an inward-facing, apo state and an amine moiety of lysine-158 located in a position equivalent to the sodium ion site Na2 of LeuT. We propose that lysine-158 is central to proton-coupled transport and that the amine group serves the same functional role as the Na2 ion in LeuT, thus demonstrating common principles among proton- and sodium-coupled transporters.
Authors:
Paul L Shaffer; April Goehring; Aruna Shankaranarayanan; Eric Gouaux
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2009-07-16
Journal Detail:
Title:  Science (New York, N.Y.)     Volume:  325     ISSN:  1095-9203     ISO Abbreviation:  Science     Publication Date:  2009 Aug 
Date Detail:
Created Date:  2009-08-21     Completed Date:  2009-09-02     Revised Date:  2014-09-24    
Medline Journal Info:
Nlm Unique ID:  0404511     Medline TA:  Science     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1010-4     Citation Subset:  IM    
Data Bank Information
Bank Name/Acc. No.:
PDB/3GI8;  3GI9;  3GIA
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acid Transport Systems / chemistry*,  metabolism*
Amino Acids / metabolism
Antiporters / chemistry
Apoproteins / chemistry,  metabolism
Archaeal Proteins / chemistry*,  metabolism*
Crystallization
Crystallography, X-Ray
Escherichia coli Proteins / chemistry
Methanococcus / chemistry*
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Folding
Protein Structure, Secondary
Protons
Sodium / metabolism
Substrate Specificity
Grant Support
ID/Acronym/Agency:
R01 MH070039/MH/NIMH NIH HHS; R01 MH070039-05/MH/NIMH NIH HHS; T32 GM008281/GM/NIGMS NIH HHS; T32 GM008281-17/GM/NIGMS NIH HHS; U54 GM075026/GM/NIGMS NIH HHS; U54 GM075026-040002/GM/NIGMS NIH HHS; //Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/Amino Acid Transport Systems; 0/Amino Acids; 0/Antiporters; 0/Apoproteins; 0/Archaeal Proteins; 0/Escherichia coli Proteins; 0/Protons; 0/YjdE protein, E coli; 9NEZ333N27/Sodium
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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