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Structure paper

TitleInsights into the mechanism of pyrrole polymerization catalysed by porphobilinogen deaminase: high-resolution X-ray studies of the Arabidopsis thaliana enzyme.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 69, Page 471-485, Year 2013
Publish dateNov 1, 2012 (structure data deposition date)
AuthorsRoberts, A. / Gill, R. / Hussey, R.J. / Mikolajek, H. / Erskine, P.T. / Cooper, J.B. / Wood, S.P. / Chrystal, E.J. / Shoolingin-Jordan, P.M.
External linksActa Crystallogr. ,Sect. D / PubMed:23519422
MethodsX-ray diffraction
Resolution1.45 Å
Structure data

PDB-4htg:
Porphobilinogen Deaminase from Arabidopsis Thaliana
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

Chemicals

ChemComp-18W:
3-[(5Z)-5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methylidene}-4-(carboxymethyl)-2-oxo-2,5-dihydro-1H-pyrrol-3-yl]propanoic acid

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • arabidopsis thaliana (thale cress)
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / Type-II periplasmic binding protein fold / Porphyrin binding / Tetrapyrrole biosynthesis / Porphobilinogen (porphyrin) binding / Chloroplast / TRANSFERASE-TRANSFERASE INHIBITOR complex

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