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PDBsum entry 2pv7

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protein ligands Protein-protein interface(s) links
Isomerase, oxidoreductase PDB id
2pv7
Jmol
Contents
Protein chains
276 a.a. *
Ligands
TYR ×2
NAD ×2
Waters ×393
* Residue conservation analysis
PDB id:
2pv7
Name: Isomerase, oxidoreductase
Title: Crystal structure of chorismate mutase / prephenate dehydrog (tyra) (1574749) from haemophilus influenzae rd at 2.00 a r
Structure: T-protein [includes: chorismate mutase (ec 5.4.99 and prephenate dehydrogenase (ec 1.3.1.12) (pdh)]. Chain: a, b. Fragment: residues 81-377. Engineered: yes
Source: Haemophilus influenzae. Organism_taxid: 727. Strain: rd, dsm 11121, kw20. Atcc: 51907. Gene: 1574749, tyra, hi1290. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.163     R-free:   0.194
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref: H.J.Chiu et al. (2010). The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 1317-1325. PubMed id: 20944228
Date:
09-May-07     Release date:   22-May-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P43902  (TYRA_HAEIN) -  T-protein
Seq:
Struc:
377 a.a.
276 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: E.C.1.3.1.12  - Prephenate dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Phenylalanine and Tyrosine Biosynthesis
      Reaction: Prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH
Prephenate
+
NAD(+)
Bound ligand (Het Group name = NAD)
corresponds exactly
=
4-hydroxyphenylpyruvate
Bound ligand (Het Group name = TYR)
matches with 85.71% similarity
+ CO(2)
+ NADH
   Enzyme class 2: E.C.5.4.99.5  - Chorismate mutase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
      Reaction: Chorismate = prephenate
Chorismate
=
prephenate
Bound ligand (Het Group name = TYR)
matches with 70.59% similarity
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     prephenate dehydrogenase (NADP+) activity     2 terms  

 

 
    reference    
 
 
Acta Crystallogr Sect F Struct Biol Cryst Commun 66:1317-1325 (2010)
PubMed id: 20944228  
 
 
The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes.
H.J.Chiu, P.Abdubek, T.Astakhova, H.L.Axelrod, D.Carlton, T.Clayton, D.Das, M.C.Deller, L.Duan, J.Feuerhelm, J.C.Grant, A.Grzechnik, G.W.Han, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, P.Kozbial, S.S.Krishna, A.Kumar, D.Marciano, D.McMullan, M.D.Miller, A.T.Morse, E.Nigoghossian, L.Okach, R.Reyes, H.J.Tien, C.B.Trame, H.van den Bedem, D.Weekes, Q.Xu, K.O.Hodgson, J.Wooley, M.A.Elsliger, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson.
 
  ABSTRACT  
 
No abstract given.