PDBsum entry 6hcl

Membrane protein

PDB id: 6hcl

Contents

Protein chains

395 a.a.

366 a.a.

Ligands

2OP ×3

BNG

PDB id:

6hcl

Name:

Membrane protein

Title:

Crystal structure of a mfs transporter with ligand at 2.69 angstroem resolution

Structure:

Major facilitator superfamily mfs_1. Chain: a, b. Engineered: yes

Source:

Syntrophobacter fumaroxidans mpob. Organism_taxid: 335543. Gene: sfum_3364. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.50Å R-factor: 0.240 R-free: 0.259

Authors:

D.Kalbermatter,P.Bosshart,S.Bonetti,D.Fotiadis

Key ref:

P.D.Bosshart et al. (2019). Mechanistic basis of L-lactate transport in the SLC16 solute carrier family. Nat Commun, 10, 2649. PubMed id: 31201333 DOI: 10.1038/s41467-019-10566-6

Date:

15-Aug-18 Release date: 03-Jul-19

Protein chain

A0LNN5  (A0LNN5_SYNFM) -  L-lactate transporter from Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB)

Seq: 412 a.a.

Struc: 395 a.a.

Protein chain

A0LNN5  (A0LNN5_SYNFM) -  L-lactate transporter from Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB)

Seq: 412 a.a.

Struc: 366 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1038/s41467-019-10566-6

Nat Commun 10:2649 (2019)

PubMed id: 31201333

Mechanistic basis of L-lactate transport in the SLC16 solute carrier family.

P.D.Bosshart, D.Kalbermatter, S.Bonetti, D.Fotiadis.

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.