 | Figure 1
Nature Structural Biology
9, 563 - 564 (2002)
doi:10.1038/nsb0802-563
Last, but not leastPhilip Matsumura | | | | Figure 1. Schematic view of the helix-turn-helix hairpin of CheZ.
In the CheZ dimer, the hairpins in each subunit flair away
from each other, leaving them free to interact with other proteins. The
hydrophobic residues of the two amphipathic helices face inward and polar
groups face outward, except that there are several exposed hydrophobic residues
in or adjacent to the loop. The phenotypes of mutations affecting different
regions of this structure, which includes residues 83−121, are indicated
by different shadings, as shown in the figure. All of the mutated residues that
impair chemotaxis are located at the helix−helix packing face or the
subunit interface.
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