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 5
Octyl-β-D-glucoside binding and crystal packing. (a) Top, the packing of molecules around the crystallographic threefold axis with adjacent molecules in the lattice depicted as translucent ribbons coloured by chain. βOG1 and βOG2 are shown in cylinder format with C atoms in grey and O atoms in red. Bottom, packing of molecules around the crystallographic fourfold axis with βOG3 molecules represented as above. (b) Detail of the binding of βOG1 and βOG2. Residues surrounding the glycolipid are shown in ball-and-stick format coloured as above except that C atoms are shown in green for one VapD molecule and in light blue for its symmetry mate. Selected residues are labelled. Residues from the symmetry-related molecule are indicated by primes (′). Polar interactions are indicated by dashed lines.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

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

doi:10.1107/S1399004714012632

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