PDBsum entry 4llh

Transport protein

PDB id: 4llh

Contents

Protein chains

524 a.a.

492 a.a.

Ligands

1Y8 ×3

CM5 ×2

Metals

_NA ×2

_CL

Waters ×91

PDB id:

4llh

Name:

Transport protein

Title:

Substrate bound outward-open state of the symporter betp

Structure:

Glycine betaine transporter betp. Chain: a, b, c. Fragment: unp residues 30-595. Engineered: yes. Mutation: yes

Source:

Corynebacterium glutamicum. Organism_taxid: 196627. Strain: atcc 13032 / dsm 20300 / jcm 1318 / lmg 3730 / ncimb 10025. Gene: betp, cgl0892, cg1016. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.80Å R-factor: 0.243 R-free: 0.290

Authors:

C.Perez,B.Faust,C.Ziegler

Key ref:

C.Perez et al. (2014). Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na+ coupling. Nat Commun, 5, 4231. PubMed id: 25023443 DOI: 10.1038/ncomms5231

Date:

09-Jul-13 Release date: 07-May-14

Protein chain

P54582  (BETP_CORGL) -  Glycine betaine transporter BetP from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)

Seq: 595 a.a.

Struc: 524 a.a.*

Protein chains

P54582  (BETP_CORGL) -  Glycine betaine transporter BetP from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)

Seq: 595 a.a.

Struc: 492 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C: E.C.?

DOI no: 10.1038/ncomms5231

Nat Commun 5:4231 (2014)

PubMed id: 25023443

Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na+ coupling.

C.Perez, B.Faust, A.R.Mehdipour, K.A.Francesconi, L.R.Forrest, C.Ziegler.

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.