Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis

Rodarte, J.V.; Abendroth, J.; Edwards, T.E.; Lorimer, D.D.; Staker, B.L.; Zhang, S.; Myler, P.J.; McLaughlin, K.J.

doi:10.1107/S2053230X21001497

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 2
Crystal structure of R. felis acetoacetyl-CoA reductase. (a) Ribbon diagram of the R. felis acetoacetyl-CoA reductase tetramer. Helices are colored in magenta and strands in green, with a representative monomer highlighted in violet. Acetoacetyl-CoA reductase crystallized with two molecules per asymmetric unit, and a tetramer was generated by crystallographic symmetry. (b) Representative monomer of R. felis acetoacetyl-CoA reductase with secondary-structure elements labeled. The active-site residues (Ser135, Tyr148 and Lys152) are grouped in helix α6 and the connecting loop to β5.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 77| Part 2| February 2021| Pages 54-60

https://doi.org/10.1107/S2053230X21001497

Follow Acta Cryst. F

Search IUCr Journals		doi		Advanced search
Author		volume	page