1F6Y

MAD CRYSTAL STRUCTURE ANALYSIS OF METHYLTETRAHYDROFOLATE: CORRINOID/IRON-SULFUR PROTEIN METHYLTRANSFERASE (METR)

Summary for 1F6Y

• Entry DOI: 10.2210/pdb1f6y/pdb
• Related: 1ad1 1ad4 1aj0 1aj2 1ajz
• Descriptor: 5-METHYLTETRAHYDROFOLATE CORRINOID/IRON SULFUR PROTEIN METHYLTRANSFERASE (2 entities in total)
• Functional Keywords: carbon dioxide fixation, cobalamin, methyltatrahydrofolate, methyltransferase, one-carbon metabolism, tim barrel, homodimer, transferase
• Biological source: Moorella thermoacetica
• Total number of polymer chains: 2
• Total formula weight: 57340.46

Authors

Doukov, T.I.,Seravalli, J.,Stezowski, J.J.,Ragsdale, S.W. (deposition date: 2000-06-23, release date: 2000-08-31, Last modification date: 2024-02-07)

Primary citation

Doukov, T.,Seravalli, J.,Stezowski, J.J.,Ragsdale, S.W.
Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase.
Structure Fold.Des., 8:817-830, 2000

PubMed Abstract: Methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr), catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide center in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin. We report the first structure of a protein in this family.

PubMed: 10997901
DOI: 10.1016/S0969-2126(00)00172-6

Experimental method

X-RAY DIFFRACTION (2.2 Å)