Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution

Azim, N.; Deery, E.; Warren, M.J.; Wolfenden, B.A.A.; Erskine, P.; Cooper, J.B.; Coker, A.; Wood, S.P.; Akhtar, M.

doi:10.1107/S139900471303294X

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 4
Sequence alignment and secondary structure of B. megaterium PBGD. An alignment of B. megaterium PBGD with the enzyme from another prokaryote (E. coli) along with the plant (A. thaliana) and human enzymes. The secondary-structure elements are labelled using the notation of Louie et al. (1992

) and the amino-acid residues are colour-coded as follows: cyan, basic; red, acidic; green, neutral polar; pink, bulky hydrophobic; white, Gly, Ala and Pro; yellow, Cys.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 3| February 2014| Pages 744-751

doi:10.1107/S139900471303294X

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