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6G9X

Crystal structure of a MFS transporter at 2.54 Angstroem resolution

Summary for 6G9X
Entry DOI10.2210/pdb6g9x/pdb
DescriptorMajor facilitator superfamily MFS_1, MERCURY (II) ION, 2-sulfanylbenzoic acid, ... (6 entities in total)
Functional Keywordsmfs transporter, membrane protein
Biological sourceSyntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Total number of polymer chains2
Total formula weight94391.62
Authors
Kalbermatter, D.,Bosshart, P.,Bonetti, S.,Fotiadis, D. (deposition date: 2018-04-11, release date: 2019-07-03, Last modification date: 2024-05-08)
Primary citationBosshart, P.D.,Kalbermatter, D.,Bonetti, S.,Fotiadis, D.
Mechanistic basis of L-lactate transport in the SLC16 solute carrier family.
Nat Commun, 10:2649-2649, 2019
Cited by
PubMed Abstract: In human and other mammalian cells, transport of L-lactate across plasma membranes is mainly catalyzed by monocarboxylate transporters (MCTs) of the SLC16 solute carrier family. MCTs play an important role in cancer metabolism and are promising targets for tumor treatment. Here, we report the crystal structures of an SLC16 family homologue with two different bound ligands at 2.54 and 2.69 Å resolution. The structures show the transporter in the pharmacologically relevant outward-open conformation. Structural information together with a detailed structure-based analysis of the transport function provide important insights into the molecular working mechanisms of ligand binding and L-lactate transport.
PubMed: 31201333
DOI: 10.1038/s41467-019-10566-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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