5laa

X-RAY STRUCTURE OF THE METHYLTRANSFERASE SUBUNIT A FROM METHANOTHERMUS FERVIDUS IN COMPLEX WITH COBALAMIN

spinqualitylabelsall models 5laa, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5laa is a 3 chain structure with sequence from Methanothermus fervidus DSM 2088. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: B12 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E3GWY7_METFV Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.[HAMAP-Rule:MF_01093] Publication Abstract from PubMed In the three domains of life, vitamin B12 (cobalamin) is primarily used in methyltransferase and isomerase reactions. The methyltransferase complex MtrA-H of methanogenic archaea has a key function in energy conservation by catalysing the methyl transfer from methyl-tetrahydromethanopterin to coenzyme M and its coupling with sodium-ion translocation. The cobalamin-binding subunit MtrA is not homologous to any known B12-binding proteins and is proposed as the motor of the sodium-ion pump. Here, we present crystal structures of the soluble domain of the membrane-associated MtrA from Methanocaldococcus jannaschii and the cytoplasmic MtrA homologue/cobalamin complex from Methanothermus fervidus. The MtrA fold corresponds to the Rossmann-type alpha/beta fold, which is also found in many cobalamin-containing proteins. Surprisingly, the cobalamin-binding site of MtrA differed greatly from all the other cobalamin-binding sites. Nevertheless, the hydrogen-bond linkage at the lower axial-ligand site of cobalt was equivalently constructed to that found in other methyltransferases and mutases. A distinct polypeptide segment fixed through the hydrogen-bond linkage in the relaxed Co(III) state might be involved in propagating the energy released upon corrinoid demethylation to the sodium-translocation site by a conformational change. MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode.,Wagner T, Ermler U, Shima S Sci Rep. 2016 Jun 21;6:28226. doi: 10.1038/srep28226. PMID:27324530 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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