1GTT
CRYSTAL STRUCTURE OF HPCE
Summary for 1GTT
| Entry DOI | 10.2210/pdb1gtt/pdb |
| Related | 1I7O |
| Descriptor | 4-HYDROXYPHENYLACETATE DEGRADATION BIFUNCTIONAL ISOMERASE/DECARBOXYLASE, CALCIUM ION (3 entities in total) |
| Functional Keywords | isomerase, lyase, bifunctional enzyme, multifunctional enzyme decarboxylase, aromatic hydrocarbons catabolism |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 4 |
| Total formula weight | 188776.94 |
| Authors | Tame, J.R.H.,Namba, K.,Dodson, E.J.,Roper, D.I. (deposition date: 2002-01-18, release date: 2002-03-08, Last modification date: 2024-11-13) |
| Primary citation | Tame, J.R.H.,Namba, K.,Dodson, E.J.,Roper, D.I. The Crystal Structure of Hpce, a Bifunctional Decarboxylase/Isomerase with a Multifunctional Fold. Biochemistry, 41:2982-, 2002 Cited by PubMed Abstract: 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. PubMed: 11863436DOI: 10.1021/BI015717T PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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