Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules

Bakolitsa, C.; Xu, Q.; Rife, C.L.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Carlton, D.; Chen, C.; Chiu, H.-J.; 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.; Hodgson, K.O.; Wooley, J.; Elsliger, M.-A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.

doi:10.1107/S1744309110032999

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
Structural organization of BT_3984 and homologs. (a) Surface representation of BT_3984 showing the two interlocking regions (N-terminal subdomain, residues 31–265, in blue; C-terminal subdomain, residues 266–537, in magenta) with the binding site for N-acetyllactosamine (LacNAc, in orange ball-and-stick representation) lying across the domain interface. LacNAc was modeled from structural superposition of BT_3984 (PDB code 3cgh ; residues 31–537) with another SusD homolog, BT_1043 (PDB code 3ehn ; residues 33–546). (b) Ribbon diagram of BT_3984 in the same orientation as in (a) colored by sequence conservation according to ConSurf (Landau et al., 2005

). High conservation among BT_3984 homologs is indicated in maroon and low conservation is indicated in turquoise. The potential SusC-binding interface is indicated.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| September 2010| Pages 1274-1280

doi:10.1107/S1744309110032999

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