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![[Figure 2]](kw5140fig2mag.jpg)
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Figure 2
Structure of the T. thermophilus MS folate-binding module. (a) The crystal structure of the T. thermophilus MS Fol module is shown in cartoon mode. Helices and sheets are colored cyan and red, respectively. (b) Amino-acid alignment of the folate-binding modules of MS and MeTr. Thermus, Thermus thermophilus MS (GenBank accession No. NC_006461); E.coli, Escherichia coli MS (J04975); human, H. sapiens MS (U73338); B.thetaiotaomicron, Bacteroides thetaiotaomicron VPI-5482 MS (NC_004663); Thermotoga, Thermotoga maritima MS (NC_000853); D.hafniense, Desulfitobacterium hafniense DCB-2 methyltetrahydrofolate-corrinoid/iron–sulfur protein methyltransferase (Dhaf_0722; ACL18786); M.thermoacetica, Moorella thermoacetica 5-methyltetrahydrofolate-corrinoid/iron–sulfur protein co-methyltransferase (AcsE; Q46389). Protein portions forming helices and sheets are colored cyan and magenta, respectively. Amino-acid chains that comprise structurally undetermined regions are shown in gray. Residues conserved only in MS are highlighted in yellow and those conserved across all methyltransferases are highlighted in green. The last helix of the Fol module in T. thermotoga MS (α8F) is underlined in blue and the C-terminal region including helices α8aF, α8bF, α8cF and α8dF of T. thermophilus MS is underlined in red. The red vertical lines indicate the C-terminal ends of the expressed and crystallized protein constructs. |
![[Figure 2]](kw5140fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
