1GTT

CRYSTAL STRUCTURE OF HPCE

1GTT の概要

• エントリーDOI: 10.2210/pdb1gtt/pdb
• 関連するPDBエントリー: 1I7O
• 分子名称: 4-HYDROXYPHENYLACETATE DEGRADATION BIFUNCTIONAL ISOMERASE/DECARBOXYLASE, CALCIUM ION (3 entities in total)
• 機能のキーワード: isomerase, lyase, bifunctional enzyme, multifunctional enzyme decarboxylase, aromatic hydrocarbons catabolism
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 188776.94

構造登録者

Tame, J.R.H.,Namba, K.,Dodson, E.J.,Roper, D.I. (登録日: 2002-01-18, 公開日: 2002-03-08, 最終更新日: 2024-11-13)

主引用文献

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

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: 11863436
DOI: 10.1021/BI015717T

実験手法

X-RAY DIFFRACTION (1.7 Å)