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Fig. 7. (A) A model of one monomer of M. trossulus cMDH, based on the
structure of the pig ortholog (PDB accession number 4MDH). All residues that
differ between the M. trossulus and the M. galloprovincialis
or M. californianus orthologs are labeled; the non-conservative
mutation at position 114 is shown in dark spacefill. Representative active
site residues are shown in light spacefill, and the highly mobile catalytic
loop, which must move by
10 Å during catalysis, is black. (B) A
magnified view of mutant V114N, showing the relationship of that residue to
the catalytic loop (black), as well as the hydrogen bond that may form between
the amide nitrogen of the asparagine side chain and the carbonyl oxygen of
143Y on the neighboring helix 
1F. Models were visualized with VMD
(Humphrey et al., 1996).
