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TitleStructural and Biochemical Characterization of a Copper-Binding Mutant of the Organomercurial Lyase MerB: Insight into the Key Role of the Active Site Aspartic Acid in Hg-Carbon Bond Cleavage and Metal Binding Specificity.
Journal, issue, pagesBiochemistry, Vol. 55, Page 1070-1081, Year 2016
Publish dateJun 12, 2015 (structure data deposition date)
AuthorsWahba, H.M. / Lecoq, L. / Stevenson, M. / Mansour, A. / Cappadocia, L. / Lafrance-Vanasse, J. / Wilkinson, K.J. / Sygusch, J. / Wilcox, D.E. / Omichinski, J.G.
External linksBiochemistry / PubMed:26820485
MethodsX-ray diffraction
Resolution1.24 - 1.96 Å
Structure data

PDB-5c0t:
Crystal structure of the mercury-bound form of MerB mutant D99S
Method: X-RAY DIFFRACTION / Resolution: 1.96 Å

PDB-5c0u:
Crystal structure of the copper-bound form of MerB mutant D99S
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

PDB-5c17:
Crystal structure of the mercury-bound form of MerB2
Method: X-RAY DIFFRACTION / Resolution: 1.24 Å

PDB-5dsf:
Crystal structure of the mercury-bound form of MerB mutant D99S
Method: X-RAY DIFFRACTION / Resolution: 1.954 Å

Chemicals

ChemComp-HG:
Unknown entry

ChemComp-BR:
BROMIDE ION

ChemComp-HOH:
WATER

ChemComp-CU:
COPPER (II) ION

ChemComp-GOL:
GLYCEROL

ChemComp-DTV:
(2S,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL

Source
  • escherichia coli (E. coli)
  • bacillus megaterium (bacteria)
KeywordsLYASE / METAL BINDING PROTEIN / Bacterial Proteins / Cysteine / Escherichia coli / Lyases / Mercury / Mutation / copper

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