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Structure paper

TitleStructural 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.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 744-751, Year 2014
Publish dateSep 6, 2013 (structure data deposition date)
AuthorsAzim, N. / Deery, E. / Warren, M.J. / Wolfenden, B.A. / Erskine, P. / Cooper, J.B. / Coker, A. / Wood, S.P. / Akhtar, M.
External linksActa Crystallogr. ,Sect. D / PubMed:24598743
MethodsX-ray diffraction
Resolution1.455 - 1.6 Å
Structure data

PDB-4mlq:
Crystal structure of Bacillus megaterium porphobilinogen deaminase
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-4mlv:
Crystal Structure of Bacillus megaterium porphobilinogen deaminase
Method: X-RAY DIFFRACTION / Resolution: 1.455 Å

Chemicals

ChemComp-DPM:
3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1H-pyrrol-3-yl]propanoic acid

ChemComp-29P:
3-[(5S)-5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-2-oxo-2,5-dihydro-1H-pyrrol-3-yl]propanoic acid

ChemComp-ACY:
ACETIC ACID

ChemComp-HOH:
WATER

Source
  • bacillus megaterium (bacteria)
KeywordsTRANSFERASE / tetrapyrrole biosynthesis / porphobilinogen deaminase / dipyrromethane cofactor / three-domain fold / domains 1 and 2 resemble the fold of type II periplasmic binding proteins / pyrrole polymerisation

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