Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs

Geerds, C.; Wohlmann, J.; Haas, A.; Niemann, H.H.

doi:10.1107/S2053230X14009911

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
(a) Cartoon representation of VapB coloured from dark blue to red from the N-terminus to the C-terminus. The two views are rotated 180° around a vertical axis. (b) Electrostatic potential of VapB oriented as in (a) and coloured on a scale from −15 (red) to +15 (blue) kT/e. (c) Distribution of hydrophilic (left) and hydrophobic (right) residues in VapB oriented as in the left of (a).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 70| Part 7| July 2014| Pages 866-871

https://doi.org/10.1107/S2053230X14009911

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