4UVM

In meso crystal structure of the POT family transporter PepTSo

Summary for 4UVM

• Entry DOI: 10.2210/pdb4uvm/pdb
• Descriptor: GLUTATHIONE UPTAKE TRANSPORTER, (2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE, (2R)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE, ... (4 entities in total)
• Functional Keywords: transport protein, major facillitator superfamily, proton oligopeptide transporter (pot) family, peptide transporter
• Biological source: SHEWANELLA ONEIDENSIS
• Total number of polymer chains: 1
• Total formula weight: 59257.12

Authors

Lyons, J.A.,Solcan, N.,Caffrey, M.,Newstead, S. (deposition date: 2014-08-07, release date: 2015-02-04, Last modification date: 2024-01-10)

Primary citation

Fowler, P.W.,Orwick-Rydmark, M.,Radestock, S.,Solcan, N.,Dijkman, P.M.,Lyons, J.A.,Kwok, J.,Caffrey, M.,Watts, A.,Forrest, L.R.,Newstead, S.
Gating Topology of the Proton-Coupled Oligopeptide Symporters.
Structure, 23:290-, 2015

PubMed Abstract: Proton-coupled oligopeptide transporters belong to the major facilitator superfamily (MFS) of membrane transporters. Recent crystal structures suggest the MFS fold facilitates transport through rearrangement of their two six-helix bundles around a central ligand binding site; how this is achieved, however, is poorly understood. Using modeling, molecular dynamics, crystallography, functional assays, and site-directed spin labeling combined with double electron-electron resonance (DEER) spectroscopy, we present a detailed study of the transport dynamics of two bacterial oligopeptide transporters, PepTSo and PepTSt. Our results identify several salt bridges that stabilize outward-facing conformations and we show that, for all the current structures of MFS transporters, the first two helices of each of the four inverted-topology repeat units form half of either the periplasmic or cytoplasmic gate and that these function cooperatively in a scissor-like motion to control access to the peptide binding site during transport.

PubMed: 25651061
DOI: 10.1016/J.STR.2014.12.012

Experimental method

X-RAY DIFFRACTION (3 Å)