The structure of the first representative of Pfam family PF09836 reveals a two-domain organization and suggests involvement in transcriptional regulation

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

doi:10.1107/S1744309109022672

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
NGO1945 dimerization. Based on crystal-packing analysis, dimerization may occur via (a) N-terminal domain helices H1, H5 and H7, with a total buried surface area of 1550 Å² (red), or (b) C-terminal domain helices H8, H9 and H11, with a total buried surface area of 1930 Å² (gray) (for clarity, the monomer encircled by a dashed oval is depicted in approximately the same orientation in both panels).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| October 2010| Pages 1174-1181

doi:10.1107/S1744309109022672

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