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 2
Structural comparison between YP_749275.1 and YP_001095227.1. (a) Superposition of the two structures underscores their overall similarity. The major differences arise from the different relative positions and orientations of helices α2 and α3. These two helices in YP_749275.1 (cyan) are close together, while they separate in YP_001095227.1 (green). (b) A surface representation of YP_001095227.1 in the `open' state shows the presence of a wide cavity. The C atoms are colored grey, O atoms red and N atoms blue. The 2-methyl-2,4-pentanediol (MPD) molecules are shown as cyan and red sticks. The opening and closing of the cavity is regulated by the movement of helix α3 away from or towards α2, which involves an ∼5 Å translation and a 90° rotation of this helix. (c) YP_749275.1 reveals no cavity in the `closed' state of the protein.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309109042481

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