Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins

Meshcheryakov, V.A.; Kitao, A.; Matsunami, H.; Samatey, F.A.

doi:10.1107/S0907444913002102

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 5
Flexibility of the N-terminal α-helix of Salmonella FlhB_C observed in MD simulations. (a) Key residues and vectors used for MD analysis in Table 2

. The vectors connecting residues 229–238, 238–256, 256–264, 265–269 and 238–264 are defined as V1–V5, respectively. (b–e) Structural variations of the N-terminal α-helix during MD simulations when the globular domain is superimposed for (b) the wild-type FlhB_C, (c) FlhB_C Δ(281–285), (d) FlhB_C AAAAA_281–285 and (e) FlhB_C PPPPP_281–285. For each case, six snapshots were chosen based on the maximum and minimum values of D, θ₁₄ and χ₅ (see Table 2

for their definitions).

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 69| Part 5| April 2013| Pages 812-820

doi:10.1107/S0907444913002102

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