Structure of Bacteroides thetaiotaomicron BT2081 at 2.05 Å resolution: the first structural representative of a new protein family that may play a role in carbohydrate metabolism

Yeh, A.P.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Bakolitsa, C.; Cai, X.; Carlton, D.; Chen, C.; Chiu, H.-J.; Chiu, M.; Clayton, T.; Das, D.; Deller, M.C.; Duan, L.; Ellrott, K.; Farr, C.L.; Feuerhelm, J.; Grant, J.C.; Grzechnik, A.; Han, G.W.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Kozbial, P.; Krishna, S.S.; Kumar, A.; Lam, W.W.; Marciano, D.; McMullan, D.; Miller, M.D.; Morse, A.T.; Nigoghossian, E.; Nopakun, A.; Okach, L.; Puckett, C.; Reyes, R.; 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/S1744309110028228

Acta Crystallographica Section F
Acta Crystallographica
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Figure 1
Crystal structure of BT2081 from B. thetaiotaomicron. (a) Ribbon diagram of the BT2081 monomer, showing the distinct N-terminal (green) and C-terminal (purple) domains. Helices (H1–H7) and β-strands (β1–β28) are indicated. (b) Diagram showing the secondary-structure elements of BT2081 superimposed on its primary sequence. The labeling of secondary-structure elements [colored by domain as in (a)] is in accord with PDBsum (https://www.ebi.ac.uk/pdbsum ), in which α-helices (H1, H3, H5 and H6), 3₁₀-helices (H2, H4 and H7) and β-strands (β1–β28) are labeled sequentially, β-turns and γ-turns are designated by Greek letters (β, γ) and β-hairpins by red loops.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| August 2010| Pages 1287-1296

doi:10.1107/S1744309110028228

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