PDBsum entry 4hzu

Hydrolase, transport protein

PDB id: 4hzu

Contents

Protein chains

284 a.a.

273 a.a.

240 a.a.

164 a.a.

PDB id:

4hzu

Name:

Hydrolase, transport protein

Title:

Structure of a bacterial energy-coupling factor transporter

Structure:

Energy-coupling factor transporter atp-binding protein ecfa 1. Chain: b. Synonym: ecf transporter a component ecfa 1. Engineered: yes. Energy-coupling factor transporter atp-binding protein ecfa 2. Chain: a. Synonym: ecf transporter a component ecfa 2.

Source:

Lactobacillus brevis. Organism_taxid: 1580. Gene: ecfa1, cbio1, lvis_1661. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ecfa2, cbio2, lvis_1662. Gene: ecft, lvis_1660. Gene: lvis_2151. Expression_system_taxid: 562

Resolution:

3.53Å R-factor: 0.243 R-free: 0.292

Authors:

T.L.Wang,G.B.Fu,X.J.Pan,Y.G.Shi

Key ref:

T.Wang et al. (2013). Structure of a bacterial energy-coupling factor transporter. Nature, 497, 272-276. PubMed id: 23584587 DOI: 10.1038/nature12045

Date:

15-Nov-12 Release date: 17-Apr-13

Protein chain

Q03PY6  (ECFA2_LACBA) -  Energy-coupling factor transporter ATP-binding protein EcfA2 from Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB 947 / NCTC 947)

Seq: 290 a.a.

Struc: 284 a.a.

Protein chain

Q03PY5  (ECFA1_LACBA) -  Energy-coupling factor transporter ATP-binding protein EcfA1 from Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB 947 / NCTC 947)

Seq: 279 a.a.

Struc: 273 a.a.

Protein chain

Q03PY7  (ECFT_LACBA) -  Energy-coupling factor transporter transmembrane protein EcfT from Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB 947 / NCTC 947)

Seq: 266 a.a.

Struc: 240 a.a.

Protein chain

Q03NM0  (Q03NM0_LACBA) -  Predicted membrane protein from Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB 947 / NCTC 947)

Seq: 166 a.a.

Struc: 164 a.a.

Enzyme reactions

• Enzyme class 2: Chain A: E.C.7.-.-.-
• Enzyme class 3: Chain B: E.C.3.6.3.- - ?????
• Enzyme class 4: Chains T, S: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

DOI no: 10.1038/nature12045

Nature 497:272-276 (2013)

PubMed id: 23584587

Structure of a bacterial energy-coupling factor transporter.

T.Wang, G.Fu, X.Pan, J.Wu, X.Gong, J.Wang, Y.Shi.

ABSTRACT

The energy-coupling factor (ECF) transporters constitute a novel family of conserved membrane transporters in prokaryotes that have a similar domain organization to the ATP-binding cassette transporters. Each ECF transporter comprises a pair of cytosolic ATPases (the A and A' components, or EcfA and EcfA'), a membrane-embedded substrate-binding protein (the S component, or EcfS) and a transmembrane energy-coupling component (the T component, or EcfT) that links the EcfA-EcfA' subcomplex to EcfS. The structure and transport mechanism of the quaternary ECF transporter remain largely unknown. Here we report the crystal structure of a nucleotide-free ECF transporter from Lactobacillus brevis at a resolution of 3.5 Å. The T component has a horseshoe-shaped open architecture, with five α-helices as transmembrane segments and two cytoplasmic α-helices as coupling modules connecting to the A and A' components. Strikingly, the S component, thought to be specific for hydroxymethyl pyrimidine, lies horizontally along the lipid membrane and is bound exclusively by the five transmembrane segments and the two cytoplasmic helices of the T component. These structural features suggest a plausible working model for the transport cycle of the ECF transporters.