The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes

Chiu, H.-J.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Carlton, D.; Clayton, T.; Das, D.; Deller, M.C.; Duan, 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.; Marciano, D.; McMullan, D.; Miller, M.D.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Reyes, R.; Tien, H.J.; Trame, C.B.; 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/S1744309110021688

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 5
Multiple sequence alignment of representative TyrA enzymes. Regions around the α–β motif and L_β5–β6 are shown. Abbreviations: Hinf, Haemophilus influenzae Rd KW20; Etas, Erwinia tasmaniensis Et1/99; Ecol, Escherichia coli str. K-12 substr. MG1655; Plum, Photorhabdus luminescens subsp. laumondii TTO1; Pmul, Pasteurella multocida subsp. multocida str. Pm70; Vcho, Vibrio cholerae O1 biovar eltor str. N16961; Vpar, Vibrio parahaemolyticus RIMD 2210633; Yent, Yersinia enterocolitica subsp. enterocolitica 8081; Aful, Archaeoglobus fulgidus; Syne, Synechocystis sp. (Legrand et al., 2006