Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism

Chiu, H.-J.; Bakolitsa, C.; Skerra, A.; Lomize, A.; Carlton, D.; Miller, M.D.; Krishna, S.S.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Clayton, T.; Deller, M.C.; Duan, L.; Feuerhelm, J.; Grant, J.C.; Grzechnik, S.K.; Han, G.W.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Kozbial, P.; Kumar, A.; Marciano, D.; McMullan, D.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Paulsen, J.; Reyes, R.; Rife, C.L.; 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/S1744309109037749

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
NE1406 exhibits domain duplication. (a) Stereo ribbon diagram of the N-terminal domain (residues 24–220, blue) of NE1406 superimposed onto the C-terminal domain (residues 221–352, gray). (b) Structure-guided alignment of the N- and C-terminal domains of NE1406. Secondary-structure elements are indicated in blue and gray for the N- and C-terminal domains, respectively. Identical residues are boxed in orange and conservative substitutions in purple. Ala74 is underlined to denote the eight-residue break in the chain between Ala74 and Ser83. The missing region was not modeled owing to poor electron density and is likely to be flexible.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| December 2010| Pages 1153-1159

doi:10.1107/S1744309109037749

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