4U9P

Structure of the methanofuran/methanopterin biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii

Summary for 4U9P

• Entry DOI: 10.2210/pdb4u9p/pdb
• Descriptor: UPF0264 protein MJ1099, GLYCEROL (3 entities in total)
• Functional Keywords: methanopterin, methanofuran, unknown function
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 3
• Total formula weight: 78368.89

Authors

Bobik, T.A.,Morales, E.,Shin, A.,Cascio, D.,Sawaya, M.R.,Arbing, M.,Rasche, M.E. (deposition date: 2014-08-06, release date: 2014-11-12, Last modification date: 2023-12-27)

Primary citation

Bobik, T.A.,Morales, E.J.,Shin, A.,Cascio, D.,Sawaya, M.R.,Arbing, M.,Yeates, T.O.,Rasche, M.E.
Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii.
Acta Crystallogr.,Sect.F, 70:1472-1479, 2014

PubMed Abstract: Prior studies have indicated that MJ1099 from Methanocaldococcus jannaschii has roles in the biosynthesis of tetrahydromethanopterin and methanofuran, two key cofactors of one-carbon (C1) metabolism in diverse organisms including the methanogenic archaea. Here, the structure of MJ1099 has been solved to 1.7 Å resolution using anomalous scattering methods. The results indicate that MJ1099 is a member of the TIM-barrel superfamily and that it is a homohexamer. Bioinformatic analyses identified a potential active site that is highly conserved among MJ1099 homologs and the key amino acids involved were identified. The results presented here should guide further studies of MJ1099 including mechanistic studies and possibly the development of inhibitors that target the methanogenic archaea in the digestive tracts of humans and that are a source of the greenhouse gas methane.

PubMed: 25372812
DOI: 10.1107/S2053230X1402130X

Experimental method

X-RAY DIFFRACTION (1.7 Å)