Ontology highlight
ABSTRACT:
SUBMITTER: Chen J
PROVIDER: S-EPMC2492823 | biostudies-literature | 2008 Aug
REPOSITORIES: biostudies-literature
Chen Jia J Li Wei W Wang Mingzhu M Zhu Guangyu G Liu Dongqi D Sun Fei F Hao Ning N Li Xuemei X Rao Zihe Z Zhang Xuejun C XC
Protein science : a publication of the Protein Society 20080527 8
Dioxygenases catalyze dioxygen incorporation into various organic compounds and play a key role in the complex degradation pathway of mono- and polycyclic aromatic and hetero-aromatic compounds. Here we report the crystal structure of gentisate 1,2-dioxygenase from Silicibacter pomeroyi (GDOsp) at a 2.8 A resolution. The enzyme possessed a conserved three-dimensional structure of the bicupin family, forming a homotetramerization. However, each subunit of GDOsp unusually contained two ferrous cen ...[more]