2V5K

Class II aldolase HpcH - magnesium - oxamate complex

2V5K の概要

• エントリーDOI: 10.2210/pdb2v5k/pdb
• 関連するPDBエントリー: 2V5J
• 分子名称: 2,4-DIHYDROXYHEPT-2-ENE-1,7-DIOIC ACID ALDOLASE, MAGNESIUM ION, OXAMIC ACID, ... (5 entities in total)
• 機能のキーワード: lyase, class ii aldolase, homoprotocatechuate, aromatic degradation, aromatic hydrocarbons catabolismhomoprotocatechuate
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62687.25

構造登録者

Rea, D.,Fulop, V.,Bugg, T.D.H.,Roper, D.I. (登録日: 2007-07-06, 公開日: 2007-10-02, 最終更新日: 2023-12-13)

主引用文献

Rea, D.,Fulop, V.,Bugg, T.D.H.,Roper, D.I.
Structure and Mechanism of Hpch: A Metal Ion Dependent Class II Aldolase from the Homoprotocatechuate Degradation Pathway of Escherichia Coli.
J.Mol.Biol., 373:866-, 2007

PubMed Abstract: Microorganisms are adept at degrading chemically resistant aromatic compounds. One of the longest and most well characterized aromatic catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway of Escherichia coli. The final step involves the conversion of 4-hydroxy-2-oxo-heptane-1,7-dioate into pyruvate and succinic semialdehyde. This reaction is catalyzed by 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH), a member of the divalent metal ion dependent class II aldolase enzymes that have great biosynthetic potential. We have solved the crystal structure of HpcH in the apo form, and with magnesium and the substrate analogue oxamate bound, to 1.6 A and 2.0 A, respectively. Comparison with similar structures of the homologous 2-dehydro-3-deoxygalactarate aldolase, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues.

PubMed: 17881002
DOI: 10.1016/J.JMB.2007.06.048

実験手法

X-RAY DIFFRACTION (2.2 Å)