PDBsum entry 3fvq

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
343 a.a. *
ATP ×2
_CA ×3
Waters ×522
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of the nucleotide binding domain fbpc comp 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.
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
16-Jan-09     Release date:   25-Aug-09    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q5FA19  (FBPC_NEIG1) -  Fe(3+) ions import ATP-binding protein FbpC
352 a.a.
343 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Fe(3+)-transporting ATPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O + Fe3+(Out) = ADP + phosphate + Fe3+(In)
Bound ligand (Het Group name = ATP)
corresponds exactly
+ H(2)O
+ Fe(3+)(Out)
+ phosphate
+ Fe(3+)(In)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   3 terms 
  Biological process     metabolic process   6 terms 
  Biochemical function     nucleotide binding     6 terms  


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.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
23000901 V.M.Korkhov, S.A.Mireku, and K.P.Locher (2012).
Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F.
  Nature, 490, 367-372.
PDB code: 4fi3
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