PDBsum entry 3fvq

Hydrolase

PDB id: 3fvq

Contents

Protein chains

343 a.a. *

Ligands

ATP ×2

Metals

_CA ×3

Waters ×522

* Residue conservation analysis

PDB id:

3fvq

Name:

Hydrolase

Title:

Crystal structure of the nucleotide binding domain fbpc complexed with atp

Structure:

Fe(3+) ions import atp-binding protein fbpc. Chain: a, b. Engineered: yes

Source:

Neisseria gonorrhoeae. Organism_taxid: 242231. Gene: fbpc, ngo0215. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.90Å R-factor: 0.198 R-free: 0.256

Authors:

S.Newstead,P.Bilton,E.P.Carpenter,D.Campopiano,S.Iwata

Key ref:

S.Newstead et al. (2009). Insights into how nucleotide-binding domains power ABC transport. Structure, 17, 1213-1222. PubMed id: 19748342

Date:

16-Jan-09 Release date: 25-Aug-09

Protein chains

Q5FA19  (FBPC_NEIG1) -  Fe(3+) ions import ATP-binding protein FbpC from Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)

Seq: 352 a.a.

Struc: 343 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.7.2.2.7 - ABC-type Fe(3+) transporter.
• Reaction: Fe³⁺(out) + ATP + H2O = Fe³⁺(in) + ADP + phosphate + H⁺

Fe(3+)(out) (Bound ligand (Het Group name = ATP) corresponds exactly) + ATP + H2O = Fe(3+)(in) + ADP + phosphate + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Structure 17:1213-1222 (2009)

PubMed id: 19748342

Insights into how nucleotide-binding domains power ABC transport.

S.Newstead, P.W.Fowler, P.Bilton, E.P.Carpenter, P.J.Sadler, D.J.Campopiano, M.S.Sansom, S.Iwata.

ABSTRACT

The mechanism by which nucleotide-binding domains (NBDs) of ABC transporters power the transport of substrates across cell membranes is currently unclear. Here we report the crystal structure of an NBD, FbpC, from the Neisseria gonorrhoeae ferric iron uptake transporter with an unusual and substantial domain swap in the C-terminal regulatory domain. This entanglement suggests that FbpC is unable to open to the same extent as the homologous protein MalK. Using molecular dynamics we demonstrate that this is not the case: both NBDs open rapidly once ATP is removed. We conclude from this result that the closed structures of FbpC and MalK have higher free energies than their respective open states. This result has important implications for our understanding of the mechanism of power generation in ABC transporters, because the unwinding of this free energy ensures that the opening of these two NBDs is also powered.