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

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 3
Dimerization modes. (a) Monomers in YP_749275.1 assemble with β-sheets lining up side by side to form a large, extended β-sheet. (b) YP_001095227.1 has a different dimerization mode with a more limited buried surface area. (c) Possible alternate mode of dimer formation in YP_001095227.1. Helices α2 and α3 are labeled.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309109042481

Follow Acta Cryst. F

Search term		doi		Advanced search
Author		volume	page