Structure of the virulence-associated protein VapD from the intracellular pathogen Rhodococcus equi

Whittingham, J.L.; Blagova, E.V.; Finn, C.E.; Luo, H.; Miranda-CasoLuengo, R.; Turkenburg, J.P.; Leech, A.P.; Walton, P.H.; Murzin, A.G.; Meijer, W.G.; Wilkinson, A.J.

doi:10.1107/S1399004714012632

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 7
VapD and internal symmetry. VapD molecules are shown in worm representation with residues 29–77 coloured blue and residues 89–134 coloured red; the remaining residues are in grey. The C^α atoms of residues 29–77 of one molecule were superimposed onto residues 89–134 of a copy of this molecule using the SSM Superpose routine implemented in CCP4mg. (a, b) Views of VapD showing the orientation of the molecules before and after superposition and the direction of the screw axis that relates them. (c) The pair of superposed VapD molecules.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 8| July 2014| Pages 2139-2151

doi:10.1107/S1399004714012632

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