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Figure 3.
Figure 3. Ribbon representations of the HsMFE-2(dDhSCP-2LD)
dimer. (a) The upper image shows the four-helix bundle
dimerization motif of hydratase 2 formed by the a-helices a1,
a5, a1' and a5' as well as the two salt bridges formed between
Glu366 and Arg506 (side-chains shown as ball-and-stick
representations). The arrows point to the active sites with
catalytic Asp510 and His515 also shown as magenta. The N and
C-domains are colored as in Figure 2(b). Note that the flexible
loops I-III are fragmented in the lower subunit (subunit J in
the crystal structure of HsMFE-2(dDhSCP-2LD)). The lower image
shows a close-up of the salt bridge Glu366-Arg506. (b) The upper
image shows the dimer after a 90° rotation around the
vertical axis of the upper image of (a). The side-chains of
Asn457 and Tyr347 are shown as ball-and-stick representations,
and the active sites of the human hydratase 2 dimer are
indicated by black arrows. The lower image shows in detail the
interactions of a2 with a1 and with the N-domain b-sheet layer.
The connections shown are described in detail in Discussion.
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