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
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 4
Conserved residues in YP_749275.1 and YP_001095227.1. (a) A sequence alignment with other members of the PFAM PB000640 family (not shown) reveals several conserved residues (marked in grey boxes). Residues from the binding cavity are colored blue and residues that are predicted to penetrate to the lipid bilayer are colored red. These residues are indicated on the structure in (b) for YP_001095227.1 and (c) for YP_749275.1. The main cluster of conserved residues from strand β1 and helices α1 and α2 is shown in purple. The protein backbone is shown in a cartoon representation. The calculated membrane boundary is shown by grey dots. A few additional nonconserved residues involved in hydrophobic interactions (Leu8, Leu74 and Trp65) in YP_749275.1 are shown in orange.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309109042481

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