Schistosoma mansoni venom allergen-like protein 4 (SmVAL4) is a novel lipid-binding SCP/TAPS protein that lacks the prototypical CAP motifs

Kelleher, A.; Darwiche, R.; Rezende, W.C.; Farias, L.P.; Leite, L.C.C.; Schneiter, R.; Asojo, O.A.

doi:10.1107/S1399004714013315

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 6
The calveolin-binding motif. (a) The conserved calveolin-binding motif (CBM) is evident in the alignment of the sequences of SmVAL4, GAPR1, Pry1 and Pry2. The secondary-structural elements shown are for SmVAL4 and GAPR1 (PDB entry 4aiw ). The location of the CBM is identified with a blue line, while the CRISP1 motif is shown as a red line. The figure was generated using EsPript and ClustalW and structural elements are labeled as described in Fig. 2

. (b) The superposed ribbon structures of SmVAL4 (gray) and GAPR1 (cyan) reveals the conformational flexibility of the CBM (shown in stick representation and identified with a blue arrow). The inositol hexakisphosphate (IP6) that was co-crystallized with GAPR1 is shown in a cyan stick representation. (c) Close-up of the superposed CBM showing the conformational difference of the loops.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 8| July 2014| Pages 2186-2196

doi:10.1107/S1399004714013315

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