PDBsum entry 1h1t

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Transferase PDB id
Protein chains
158 a.a. *
SO4 ×4
Waters ×286
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Phosphopantetheine adenylyltransferase in complex with coenzyme a from escherichia coli
Structure: Phosphopantetheine adenylyltransferase. Chain: a, b. Synonym: pantetheine-phosphate adenylyltransferase, ppat, dephospho-coa pyrophosphorylase. Ec:
Source: Escherichia coli. Organism_taxid: 562
Biol. unit: Hexamer (from PDB file)
1.78Å     R-factor:   0.218     R-free:   0.241
Authors: T.Izard
Key ref: T.Izard (2003). A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A. J Bacteriol, 185, 4074-4080. PubMed id: 12837781
21-Jul-02     Release date:   07-Jul-03    
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Protein chains
Pfam   ArchSchema ?
P0A6I6  (COAD_ECOLI) -  Phosphopantetheine adenylyltransferase
159 a.a.
158 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

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

Coenzyme A Biosynthesis (late stages)
      Reaction: ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
Bound ligand (Het Group name = COA)
matches with 51.00% 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  


J Bacteriol 185:4074-4080 (2003)
PubMed id: 12837781  
A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A.
Phosphopantetheine adenylyltransferase (PPAT) regulates the key penultimate step in the essential coenzyme A (CoA) biosynthetic pathway. PPAT catalyzes the reversible transfer of an adenylyl group from Mg(2+):ATP to 4'-phosphopantetheine to form 3'-dephospho-CoA (dPCoA) and pyrophosphate. The high-resolution crystal structure of PPAT complexed with CoA has been determined. Remarkably, CoA and the product dPCoA bind to the active site in distinct ways. Although the phosphate moiety within the phosphopantetheine arm overlaps, the pantetheine arm binds to the same pocket in two distinct conformations, and the adenylyl moieties of these two ligands have distinct binding sites. Moreover, the PPAT:CoA crystal structure confirms the asymmetry of binding to the two trimers within the hexameric enzyme. Specifically, the pantetheine arm of CoA bound to one protomer within the asymmetric unit displays the dPCoA-like conformation with the adenylyl moiety disordered, whereas CoA binds the twofold-related protomer in an ordered and unique fashion.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21527250 C.S.Cheng, C.H.Chen, Y.C.Luo, W.T.Chen, S.Y.Chang, P.C.Lyu, M.C.Kao, and H.S.Yin (2011).
Crystal structure and biophysical characterisation of Helicobacter pylori phosphopantetheine adenylyltransferase.
  Biochem Biophys Res Commun, 408, 356-361.  
20486930 J.R.Miller, V.Thanabal, M.M.Melnick, M.Lall, C.Donovan, R.W.Sarver, D.Y.Lee, J.Ohren, and D.Emerson (2010).
The use of biochemical and biophysical tools for triage of high-throughput screening hits - A case study with Escherichia coli phosphopantetheine adenylyltransferase.
  Chem Biol Drug Des, 75, 444-454.  
17873050 J.R.Miller, J.Ohren, R.W.Sarver, W.T.Mueller, Dreu, H.Case, and V.Thanabal (2007).
Phosphopantetheine adenylyltransferase from Escherichia coli: investigation of the kinetic mechanism and role in regulation of coenzyme A biosynthesis.
  J Bacteriol, 189, 8196-8205.  
16606823 C.Yuan, C.J.Rieke, G.Rimon, B.A.Wingerd, and W.L.Smith (2006).
Partnering between monomers of cyclooxygenase-2 homodimers.
  Proc Natl Acad Sci U S A, 103, 6142-6147.  
  17077496 J.Y.Kang, H.H.Lee, H.J.Yoon, H.S.Kim, and S.W.Suh (2006).
Overexpression, crystallization and preliminary X-ray crystallographic analysis of phosphopantetheine adenylyltransferase from Enterococcus faecalis.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1131-1133.  
15322293 V.K.Morris, and T.Izard (2004).
Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
  Protein Sci, 13, 2547-2552.
PDB code: 1tfu
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.