4MLQ

Crystal structure of Bacillus megaterium porphobilinogen deaminase

Summary for 4MLQ

• Entry DOI: 10.2210/pdb4mlq/pdb
• Related: 1PDA 4HTG
• Descriptor: Porphobilinogen deaminase, 3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1H-pyrrol-3-yl]propanoic acid, 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, ... (5 entities in total)
• Functional Keywords: tetrapyrrole biosynthesis, porphobilinogen deaminase, dipyrromethane cofactor, three-domain fold, domains 1 and 2 resemble the fold of type ii periplasmic binding proteins, pyrrole polymerisation, transferase
• Biological source: Bacillus megaterium
• Total number of polymer chains: 1
• Total formula weight: 35429.65

Authors

Azim, N.,Deery, E.,Warren, M.J.,Erskine, P.,Cooper, J.B.,Coker, A.,Wood, S.P.,Akhtar, M. (deposition date: 2013-09-06, release date: 2014-04-02)

• Primary citation: Azim, N.,Deery, E.,Warren, M.J.,Wolfenden, B.A.,Erskine, P.,Cooper, J.B.,Coker, A.,Wood, S.P.,Akhtar, M.; 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.; Acta Crystallogr.,Sect.D, 70:744-751, 2014; PubMed: 24598743; DOI: 10.1107/S139900471303294X

Experimental method

X-RAY DIFFRACTION (1.6 Å)