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 3
Active site of HinfPDDH. (a) Final model of tyrosine and NAD⁺ molecules fitted in 2F_o − F_c electron-density maps prior to model building as output from the last step of XSOLVE (JCSG, unpublished work). The map is contoured at 1σ. (b) Active site of HinfPDDH showing key active-site residues and the bound tyrosine and NAD⁺ molecules in ball-and-stick representation. C atoms are colored gray for the protein and yellow for the ligands; O, N and phosphate atoms are colored red, blue and orange, respectively.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| July 2010| Pages 1317-1325

doi:10.1107/S1744309110021688

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