Structure of a membrane-attack complex/perforin (MACPF) family protein from the human gut symbiont Bacteroides thetaiotaomicron

Xu, Q.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Bakolitsa, C.; Cai, X.; 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.; 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.; Yeh, A.; Zhou, J.; Hodgson, K.O.; Wooley, J.; Elsliger, M.-A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.

doi:10.1107/S1744309110023055

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
Multiple sequence alignment of Bth-MACPF homologs (sequence identity <90%) with the same domain architecture. The sequence numbering and secondary-structure elements of Bth-MACPF are shown at the top and domain boundaries (¶) and sequence motifs are shown at the bottom. Charged residues are highlighted in red (negative) and blue (positive), hydrophobic residues in green and hydrophilic residues in yellow. The following sequences are shown: b.th1, B. thetaiotaomicron BT_3439 (Bth-MACPF); b.sp, Bacteroides sp. 2_2_4 (UniProt accession C3QVE5); b.th2, B. thetaiotaomicron BT_3437; b.pl, B. plebeius DSM 17135 (UniProt accession B5CX96); p.en, P. endodontalis ATCC 35406 (UniProt accession C3J7W9).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| July 2010| Pages 1297-1305

doi:10.1107/S1744309110023055

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