6yu3: Difference between revisions
New page: '''Unreleased structure''' The entry 6yu3 is ON HOLD Authors: Focht, D., Neumann, C., Lyons, J., Eguskiza Bilbao, A., Blunck, R., Malinauskaite, L., Schwarz, I.O., Javitch, J.A., Quick,... |
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The | ==Crystal structure of MhsT in complex with L-phenylalanine== | ||
<StructureSection load='6yu3' size='340' side='right'caption='[[6yu3]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6yu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans Alkalihalobacillus halodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YU3 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=SOG:2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>SOG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6yu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yu3 OCA], [https://pdbe.org/6yu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yu3 RCSB], [https://www.ebi.ac.uk/pdbsum/6yu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yu3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9KDT3_HALH5 Q9KDT3_HALH5] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
MhsT of Bacillus halodurans is a transporter of hydrophobic amino acids and a homologue of the eukaryotic SLC6 family of Na(+) -dependent symporters for amino acids, neurotransmitters, osmolytes, or creatine. The broad range of transported amino acids by MhsT prompted the investigation of the substrate recognition mechanism. Here, we report six new substrate-bound structures of MhsT, which, in conjunction with functional studies, reveal how the flexibility of a Gly-Met-Gly (GMG) motif in the unwound region of transmembrane segment 6 (TM6) is central for the recognition of substrates of different size by tailoring the binding site shape and volume. MhsT mutants, harboring substitutions within the unwound GMG loop and substrate binding pocket that mimick the binding sites of eukaryotic SLC6A18/B0AT3 and SLC6A19/B0AT1 transporters of neutral amino acids, exhibited impaired transport of aromatic amino acids that require a large binding site volume. Conservation of a general (G/A/C)PhiG motif among eukaryotic members of SLC6 family suggests a role for this loop in a common mechanism for substrate recognition and translocation by SLC6 transporters of broad substrate specificity. | |||
A non-helical region in transmembrane helix 6 of hydrophobic amino acid transporter MhsT mediates substrate recognition.,Focht D, Neumann C, Lyons J, Eguskiza Bilbao A, Blunck R, Malinauskaite L, Schwarz IO, Javitch JA, Quick M, Nissen P EMBO J. 2021 Jan 4;40(1):e105164. doi: 10.15252/embj.2020105164. Epub 2020 Nov 6. PMID:33155685<ref>PMID:33155685</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6yu3" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Eguskiza Bilbao | <references/> | ||
[[Category: Focht | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Alkalihalobacillus halodurans]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Blunck R]] | ||
[[Category: | [[Category: Eguskiza Bilbao A]] | ||
[[Category: | [[Category: Focht D]] | ||
[[Category: Javitch JA]] | |||
[[Category: Lyons J]] | |||
[[Category: Malinauskaite L]] | |||
[[Category: Neumann C]] | |||
[[Category: Nissen P]] | |||
[[Category: Quick M]] | |||
[[Category: Schwarz IO]] | |||
Latest revision as of 16:35, 24 January 2024
Crystal structure of MhsT in complex with L-phenylalanineCrystal structure of MhsT in complex with L-phenylalanine
Structural highlights
FunctionPublication Abstract from PubMedMhsT of Bacillus halodurans is a transporter of hydrophobic amino acids and a homologue of the eukaryotic SLC6 family of Na(+) -dependent symporters for amino acids, neurotransmitters, osmolytes, or creatine. The broad range of transported amino acids by MhsT prompted the investigation of the substrate recognition mechanism. Here, we report six new substrate-bound structures of MhsT, which, in conjunction with functional studies, reveal how the flexibility of a Gly-Met-Gly (GMG) motif in the unwound region of transmembrane segment 6 (TM6) is central for the recognition of substrates of different size by tailoring the binding site shape and volume. MhsT mutants, harboring substitutions within the unwound GMG loop and substrate binding pocket that mimick the binding sites of eukaryotic SLC6A18/B0AT3 and SLC6A19/B0AT1 transporters of neutral amino acids, exhibited impaired transport of aromatic amino acids that require a large binding site volume. Conservation of a general (G/A/C)PhiG motif among eukaryotic members of SLC6 family suggests a role for this loop in a common mechanism for substrate recognition and translocation by SLC6 transporters of broad substrate specificity. A non-helical region in transmembrane helix 6 of hydrophobic amino acid transporter MhsT mediates substrate recognition.,Focht D, Neumann C, Lyons J, Eguskiza Bilbao A, Blunck R, Malinauskaite L, Schwarz IO, Javitch JA, Quick M, Nissen P EMBO J. 2021 Jan 4;40(1):e105164. doi: 10.15252/embj.2020105164. Epub 2020 Nov 6. PMID:33155685[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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