Open and closed conformations of two SpoIIAA-like proteins (YP_749275.1 and YP_001095227.1) provide insights into membrane association and ligand binding

Kumar, A.; Lomize, A.; Jin, K.K.; Carlton, D.; Miller, M.D.; Jaroszewski, L.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Chiu, H.-J.; Clayton, T.; Das, D.; Deller, M.C.; Duan, L.; Feuerhelm, J.; Grant, J.C.; Grzechnik, A.; Han, G.W.; Klock, H.E.; Knuth, M.W.; Kozbial, P.; Krishna, S.S.; Marciano, D.; McMullan, D.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Reyes, R.; Rife, C.L.; Sefcovic, N.; Tien, H.J.; Trame, C.B.; van den Bedem, H.; Weekes, D.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Elsliger, M.-A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.

doi:10.1107/S1744309109042481

Acta Crystallographica Section F
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Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 5
Comparison of the putative membrane association of YP_001095227.1 and YP_749275.1 with that of the CRAL-TRIO domain of human α-tocopherol transfer protein (α-TTP). (a) YP_001095227.1 in the `open' conformation (PDB code 2q3l ). (b) Dimeric form of YP_749275.1 in the `closed' conformation (PDB code 2ook ). The second molecule is colored blue and the lid helices enclosing the binding cavity are colored pink. Residues that move from the surface to the protein interior during the conformational switch are colored orange. (c) Human α-TTP in the `open' conformation (PDB code 1oiz ; Meier et al., 2003

). The N-CRAL-TRIO domain is colored yellow and the lipid-binding CRAL-TRIO domain is colored green. Molecules of detergents or bound ligands are colored in dark green here and in (d). (d) α-TTP in the `closed' conformation (PDB code 1r5l ; Min et al., 2003

). In all figures, residues that penetrate or are proposed to penetrate the lipid bilayer are colored purple. Calculated boundaries between lipid head groups and the acyl-chain region are shown by grey dots.

STRUCTURAL BIOLOGY
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ISSN: 2053-230X

Volume 66| Part 10| December 2010| Pages 1245-1253

doi:10.1107/S1744309109042481

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