4LLH

Substrate bound outward-open state of the symporter BetP

Summary for 4LLH

• Entry DOI: 10.2210/pdb4llh/pdb
• Descriptor: Glycine betaine transporter BetP, 2-(trimethyl-lambda~5~-arsanyl)ethanol, SODIUM ION, ... (6 entities in total)
• Functional Keywords: secondary transporter, transport protein
• Biological source: Corynebacterium glutamicum
• Cellular location: Cell membrane; Multi-pass membrane protein: P54582
• Total number of polymer chains: 3
• Total formula weight: 185269.66

Authors

Perez, C.,Faust, B.,Ziegler, C. (deposition date: 2013-07-09, release date: 2014-05-07, Last modification date: 2024-02-28)

Primary citation

Perez, C.,Faust, B.,Mehdipour, A.R.,Francesconi, K.A.,Forrest, L.R.,Ziegler, C.
Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na(+) coupling.
Nat Commun, 5:4231-4231, 2014

PubMed Abstract: The Na(+)-coupled betaine symporter BetP shares a highly conserved fold with other sequence unrelated secondary transporters, for example, with neurotransmitter symporters. Recently, we obtained atomic structures of BetP in distinct conformational states, which elucidated parts of its alternating-access mechanism. Here, we report a structure of BetP in a new outward-open state in complex with an anomalous scattering substrate, adding a fundamental piece to an unprecedented set of structural snapshots for a secondary transporter. In combination with molecular dynamics simulations these structural data highlight important features of the sequential formation of the substrate and sodium-binding sites, in which coordinating water molecules play a crucial role. We observe a strictly interdependent binding of betaine and sodium ions during the coupling process. All three sites undergo progressive reshaping and dehydration during the alternating-access cycle, with the most optimal coordination of all substrates found in the closed state.

PubMed: 25023443
DOI: 10.1038/ncomms5231

Experimental method

X-RAY DIFFRACTION (2.8 Å)