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 5
Superposition of B. megaterium PBGD with the Arabidopsis, E. coli and human enzymes. (a) The overall least-squares superposition of B. megaterium PBGD (cyan) with the E. coli enzyme (yellow) as well as the Arabidopsis and human enzymes (green and pink, respectively). A superposition of the four enzymes based on domain 1 alone is shown in (b), which emphasizes the different concerted shifts of domains 2 and 3 relative to domain 1 in the enzyme from each species.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

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

doi:10.1107/S139900471303294X

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