5EQN

Structure of phosphonate hydroxylase

Summary for 5EQN

• Entry DOI: 10.2210/pdb5eqn/pdb
• Descriptor: FrbJ, MAGNESIUM ION (3 entities in total)
• Functional Keywords: phosphonate hydroxylase, dioxygenases, hydrolase
• Biological source: Streptomyces rubellomurinus
• Total number of polymer chains: 2
• Total formula weight: 80806.23

Authors

Li, C.,Hu, Y.,Zhang, H. (deposition date: 2015-11-13, release date: 2016-05-18, Last modification date: 2024-11-20)

Primary citation

Li, C.,Junaid, M.,Almuqri, E.A.,Hao, S.,Zhang, H.
Structural analysis of a phosphonate hydroxylase with an access tunnel at the back of the active site.
Acta Crystallogr.,Sect.F, 72:362-368, 2016

PubMed Abstract: FrbJ is a member of the Fe(2+)/α-ketoglutarate-dependent dioxygenase family which hydroxylates the natural product FR-900098 of Streptomyces rubellomurinus, yielding the phosphonate antibiotic FR-33289. Here, the crystal structure of FrbJ, which shows structural homology to taurine dioxygenase (TauD), a key member of the same family, is reported. Unlike other members of the family, FrbJ has an unusual lid structure which consists of two β-strands with a long loop between them. To investigate the role of this lid motif, a molecular-dynamics simulation was performed with the FrbJ structure. The molecular-dynamics simulation analysis implies that the lid-loop region is highly flexible, which is consistent with the fact that FrbJ has a relatively broad spectrum of substrates with different lengths. Interestingly, an access tunnel is found at the back of the active site which connects the putative binding site of α-ketoglutarate to the solvent outside.

PubMed: 27139827
DOI: 10.1107/S2053230X16004933

Experimental method

X-RAY DIFFRACTION (2.3 Å)