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Oxidoreductase PDB id
1tg5
Jmol
Contents
Protein chain
371 a.a. *
Ligands
645
Metals
FE2
Waters ×260
* Residue conservation analysis
PDB id:
1tg5
Name: Oxidoreductase
Title: Crystal structures of plant 4-hydroxyphenylpyruvate dioxygen complexed with das645
Structure: 4-hydroxyphenylpyruvate dioxygenase. Chain: a. Synonym: 4hppd, hpd, hppdase. Engineered: yes
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: hpd, at1g06570, f12k11.9. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
Resolution:
1.90Å     R-factor:   0.191     R-free:   0.234
Authors: C.Yang,J.W.Pflugrath,D.L.Camper,M.L.Foster,D.J.Pernich,T.A.W
Key ref:
C.Yang et al. (2004). Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases. Biochemistry, 43, 10414-10423. PubMed id: 15301540 DOI: 10.1021/bi049323o
Date:
28-May-04     Release date:   17-Aug-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P93836  (HPPD_ARATH) -  4-hydroxyphenylpyruvate dioxygenase
Seq:
Struc: 		445 a.a.
371 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.13.11.27  - 4-hydroxyphenylpyruvate dioxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2
4-hydroxyphenylpyruvate
 + O(2)
 = homogentisate
 + CO(2)
      Cofactor: Iron
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   4 terms 
  Biological process     oxidation-reduction process   7 terms 
  Biochemical function     oxidoreductase activity     6 terms  

 

 
    reference    
 
 
DOI no: 10.1021/bi049323o Biochemistry 43:10414-10423 (2004)
PubMed id: 15301540  
 
 
Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases.
C.Yang, J.W.Pflugrath, D.L.Camper, M.L.Foster, D.J.Pernich, T.A.Walsh.
 
  ABSTRACT  
 
A high degree of selectivity toward the target site of the pest organism is a desirable attribute for new safer agrochemicals. To assist in the design of novel herbicides, we determined the crystal structures of the herbicidal target enzyme 4-hydroxyphenylpyruvate dioxygenase (HPPD; EC 1.13.11.27) from the plant Arabidopsis thaliana with and without an herbicidal benzoylpyrazole inhibitor that potently inhibits both plant and mammalian HPPDs. We also determined the structure of a mammalian (rat) HPPD in complex with the same nonselective inhibitor. From a screening campaign of over 1000 HPPD inhibitors, six highly plant-selective inhibitors were found. One of these had remarkable (>1600-fold) selectivity toward the plant enzyme and was cocrystallized with Arabidopsis HPPD. Detailed comparisons of the plant and mammalian HPPD-ligand structures suggest a structural basis for the high degree of plant selectivity of certain HPPD inhibitors and point to design strategies to obtain potent and selective inhibitors of plant HPPD as agrochemical leads.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19625206 P.He, and G.R.Moran (2009).
We two alone will sing: the two-substrate alpha-keto acid-dependent oxygenases.
  Curr Opin Chem Biol, 13, 443-450.  
17431691 V.Purpero, and G.R.Moran (2007).
The diverse and pervasive chemistries of the alpha-keto acid dependent enzymes.
  J Biol Inorg Chem, 12, 587-601.  
16407096 J.A.McCourt, S.S.Pang, J.King-Scott, L.W.Guddat, and R.G.Duggleby (2006).
Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase.
  Proc Natl Acad Sci U S A, 103, 569-573.
PDB codes: 1ybh 1yhy 1yhz 1yi0 1yi1 1z8n
16920789 M.L.Neidig, A.Decker, O.W.Choroba, F.Huang, M.Kavana, G.R.Moran, J.B.Spencer, and E.I.Solomon (2006).
Spectroscopic and electronic structure studies of aromatic electrophilic attack and hydrogen-atom abstraction by non-heme iron enzymes.
  Proc Natl Acad Sci U S A, 103, 12966-12973.  
16075302 D.L.Chen, and G.E.Kellogg (2005).
A computational tool to optimize ligand selectivity between two similar biomacromolecular targets.
  J Comput Aided Mol Des, 19, 69-82.  
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 codes are shown on the right.