PDBsum entry 1gtt

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protein metals Protein-protein interface(s) links
Isomerase PDB id
Protein chains
421 a.a. *
_CA ×4
Waters ×1217
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Crystal structure of hpce
Structure: 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase. Chain: a, b, c, d. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
1.7Å     R-factor:   0.217     R-free:   0.252
Authors: J.R.H.Tame,K.Namba,E.J.Dodson,D.I.Roper
Key ref:
J.R.Tame et al. (2002). The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold. Biochemistry, 41, 2982-2989. PubMed id: 11863436 DOI: 10.1021/bi015717t
18-Jan-02     Release date:   08-Mar-02    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P37352  (HPCE_ECOLX) -  Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase
427 a.a.
421 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: E.C.  - 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2
= 2-oxohept-3-enedioate
+ CO(2)
   Enzyme class 2: E.C.  - 5-carboxymethyl-2-hydroxymuconate Delta-isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 5-carboxymethyl-2-hydroxymuconate = 5-carboxy-2-oxohept-3-enedioate
= 5-carboxy-2-oxohept-3-enedioate
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     metabolic process   3 terms 
  Biochemical function     catalytic activity     6 terms  


DOI no: 10.1021/bi015717t Biochemistry 41:2982-2989 (2002)
PubMed id: 11863436  
The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold.
J.R.Tame, K.Namba, E.J.Dodson, D.I.Roper.
The structure of the bifunctional enzyme HpcE (OPET decarboxylase/HHDD isomerase) from Escherichia coli shows that the protein consists of highly similar N and C terminal halves. Sequence matches suggest that this fold is widespread among different species, including man. Many of these homologues are uncharacterized but apparently connected with the metabolism of aromatic compounds. The domain shows similar topology to the C terminal domain of fumarylacetoacetate hydrolase (FAH), a functionally related enzyme, despite lacking significant overall sequence similarity. HpcE is known to catalyze two rather different reactions, and comparisons with FAH allow some tentative conclusions to be drawn about the active sites. Key mutations within the active site apparently allow enzymes with this fold to carry out a variety chemical processes.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20233922 S.Klaffl, and B.J.Eikmanns (2010).
Genetic and functional analysis of the soluble oxaloacetate decarboxylase from Corynebacterium glutamicum.
  J Bacteriol, 192, 2604-2612.  
19187228 S.Watanabe, and K.Makino (2009).
Novel modified version of nonphosphorylated sugar metabolism--an alternative L-rhamnose pathway of Sphingomonas sp.
  FEBS J, 276, 1554-1567.  
16849334 S.J.Brouns, J.Walther, A.P.Snijders, H.J.van de Werken, H.L.Willemen, P.Worm, Vos, A.Andersson, M.Lundgren, H.F.Mazon, R.H.van den Heuvel, P.Nilsson, L.Salmon, Vos, P.C.Wright, R.Bernander, and J.van der Oost (2006).
Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment.
  J Biol Chem, 281, 27378-27388.  
  17012798 T.Adachi, A.Izumi, D.Rea, S.Y.Park, J.R.Tame, and D.I.Roper (2006).
Expression, purification and crystallization of 2-oxo-hept-4-ene-1,7-dioate hydratase (HpcG) from Escherichia coli C.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1010-1012.  
  16511168 D.Rea, V.Fülöp, T.D.Bugg, and D.I.Roper (2005).
Expression, purification and preliminary crystallographic analysis of 2,4-dihydroxy-hepta-2-ene-1,7-dioate aldolase (HpcH) from Escherichia coli C.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 821-824.  
15551868 B.A.Manjasetty, F.H.Niesen, H.Delbrück, F.Götz, V.Sievert, K.Büssow, J.Behlke, and U.Heinemann (2004).
X-ray structure of fumarylacetoacetate hydrolase family member Homo sapiens FLJ36880.
  Biol Chem, 385, 935-942.
PDB code: 1saw
12454498 A.Wright, A.Blewett, V.Fulop, R.Cooper, S.Burrows, C.Jones, and D.Roper (2002).
Expression, purification, crystallization and preliminary characterization of an HHED aldolase homologue from Escherichia coli K12.
  Acta Crystallogr D Biol Crystallogr, 58, 2191-2193.  
11914371 C.M.Nunn, S.Djordjevic, P.J.Hillas, C.R.Nishida, and P.R.Ortiz de Montellano (2002).
The crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug design.
  J Biol Chem, 277, 20033-20040.
PDB code: 1gu9
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.