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 1
Crystal structures of (a) YP_749275.1 (PDB code 2ook ) and (b) YP_001095227.1 (PDB code 2q3l ) shown as ribbon diagrams of protein monomers color-coded from the N-terminus (blue) to the C-terminus (red). Helices α1–α4 and strands β1–β5 are indicated for YP_749275.1, while every tenth residue is numbered for YP_001095227.1. (c) Diagram showing the secondary-structure elements of YP_749275.1 and YP_001095227.1 superimposed on their primary sequences. Strands and helices are indicated by arrows and coils, respectively, and labeled sequentially as β1, β2 etc. and α1, α2 etc. Identical residues in these proteins are shown in white on a red background, while similar residues are shown as the reverse (red on a white background).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309109042481

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