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 6
Superimposition of TyrA structures showing differences in the relative orientation of the N- and C-terminal domains and a close-up view of the active site of HinfPDH. (a) Superimposition of HinfPDH, AaeoPDH, AaeoPDH–Tyr–NAD⁺, SthePDH and SyneADH reveals differences in the relative orientation of the N- and C-terminal domains in these TyrA proteins. HinfPDH, AaeoPDH, AaeoPDH (monomer B)–Tyr–NAD⁺, SthePDH and SyneADH are colored green, magenta, orange, cyan and blue, respectively. (b) Same orientation as (a); for clarity, only HinfPDH and SyneADH are shown. (c) An ionic network in the active site of HinfPDH consists of Arg297, a bridging water molecule, Asp206 and Arg365′ from adjacent molecule in a dual conformation. His260, Tyr288, Gln301 and Tyr306 that could be involved in substrate selectivity are also shown. Hydrogen bonds are indicated as dashed lines.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309110021688

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