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Structure paper

TitleStructural studies of domain movement in active-site mutants of porphobilinogen deaminase from Bacillus megaterium.
Journal, issue, pagesActa Crystallogr F Struct Biol Commun, Vol. 73, Page 612-620, Year 2017
Publish dateAug 28, 2017 (structure data deposition date)
AuthorsGuo, J. / Erskine, P. / Coker, A.R. / Wood, S.P. / Cooper, J.B.
External linksActa Crystallogr F Struct Biol Commun / PubMed:29095155
MethodsX-ray diffraction
Resolution1.81 - 2.692 Å
Structure data

PDB-5ov4:
Bacillus megaterium porphobilinogen deaminase D82A mutant
Method: X-RAY DIFFRACTION / Resolution: 2.692 Å

PDB-5ov5:
Bacillus megaterium porphobilinogen deaminase D82E mutant
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

PDB-5ov6:
Bacillus megaterium porphobilinogen deaminase D82N mutant
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-HOH:
WATER

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-AWQ:
3-[4-(2-hydroxy-2-oxoethyl)-2,5-dimethyl-1~{H}-pyrrol-3-yl]propanoic acid

Source
  • bacillus megaterium (bacteria)
KeywordsTRANSFERASE / Deaminase / mutation / domain movements / cofactor / mutant

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