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PDBsum entry 3fvq

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3fvq
Jmol
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 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.
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    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q5FA19  (FBPC_NEIG1) -  Fe(3+) ions import ATP-binding protein FbpC
Seq:
Struc:
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.3.6.3.30  - Fe(3+)-transporting ATPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O + Fe3+(Out) = ADP + phosphate + Fe3+(In)
ATP
Bound ligand (Het Group name = ATP)
corresponds exactly
+ H(2)O
+ Fe(3+)(Out)
= ADP
+ 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  

 

 
    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.
 

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
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.