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Structure of the octameric enolase.

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posted on 2011-12-09, 01:10 authored by M. Judith Kornblatt, Jack A. Kornblatt, Mark A. Hancock

The identical subunits are arranged as a tetramer of A-B pairs. The color coding is: “A” subunits are green and “B” subunits are yellow. The two putative plasminogen binding sites are shown. The first: only one atom of the C-terminal lysine-433 is visible in the X-ray structure. It is coloured red. The adjacent leucine-432 is also coloured red for convenience of viewing. The second: the putative site consists of residues 248–256. It is coloured orange. Figure 1A. Top down view showing the positions of the two sites. On the A subunits, the second site is easily seen; it shows up on the B subunits when the molecule is flipped through 180°. Figure 1B. An end on view of the octamer. The orange second site is clearly exposed whereas the red C-terminal is mostly buried.