spacer
spacer

PDBsum entry 3f3m

Go to PDB code: 
protein ligands links
Transferase PDB id
3f3m
Jmol
Contents
Protein chain
155 a.a. *
Ligands
PPS
Waters ×43
* Residue conservation analysis
PDB id:
3f3m
Name: Transferase
Title: Six crystal structures of two phosphopantetheine adenylyltra reveal an alternative ligand binding mode and an associated structural change
Structure: Phosphopantetheine adenylyltransferase. Chain: a. Synonym: pantetheine-phosphate adenylyltransferase, ppat, d coa pyrophosphorylase. Engineered: yes
Source: Staphylococcus aureus. Organism_taxid: 1280. Gene: coad. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.40Å     R-factor:   0.211     R-free:   0.250
Authors: H.H.Lee,H.J.Yoon,S.W.Suh
Key ref: H.H.Lee et al. (2009). The structure of Staphylococcus aureus phosphopantetheine adenylyltransferase in complex with 3'-phosphoadenosine 5'-phosphosulfate reveals a new ligand-binding mode. Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 987-991. PubMed id: 19851003
Date:
31-Oct-08     Release date:   20-Oct-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P63820  (COAD_STAAW) -  Phosphopantetheine adenylyltransferase
Seq:
Struc:
160 a.a.
155 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.7.3  - Pantetheine-phosphate adenylyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Coenzyme A Biosynthesis (late stages)
      Reaction: ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
ATP
Bound ligand (Het Group name = PPS)
matches with 58.97% similarity
+ pantetheine 4'-phosphate
= diphosphate
+ 3'-dephospho-CoA
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     biosynthetic process   2 terms 
  Biochemical function     catalytic activity     6 terms  

 

 
    reference    
 
 
Acta Crystallogr Sect F Struct Biol Cryst Commun 65:987-991 (2009)
PubMed id: 19851003  
 
 
The structure of Staphylococcus aureus phosphopantetheine adenylyltransferase in complex with 3'-phosphoadenosine 5'-phosphosulfate reveals a new ligand-binding mode.
H.H.Lee, H.J.Yoon, J.Y.Kang, J.H.Park, d.o. .J.Kim, K.H.Choi, S.K.Lee, J.Song, H.J.Kim, S.W.Suh.
 
  ABSTRACT  
 
Bacterial phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in the coenzyme A (CoA) biosynthetic pathway. It catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to form dephospho-CoA (dPCoA) and pyrophosphate. Previous structural studies have revealed how several ligands are recognized by bacterial PPATs. ATP, ADP, Ppant and dPCoA bind to the same binding site in a highly similar manner, while CoA binds to a partially overlapping site in a different mode. To provide further structural insights into ligand binding, the crystal structure of Staphylococcus aureus PPAT was solved in a binary complex with 3'-phosphoadenosine 5'-phosphosulfate (PAPS). This study unexpectedly revealed a new mode of ligand binding to PPAT, thus providing potentially useful information for structure-based discovery of inhibitors of bacterial PPATs.