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Literature summary for 4.99.1.2 extracted from

  • Wahba, H.M.; Lecoq, L.; Stevenson, M.; Mansour, A.; Cappadocia, L.; Lafrance-Vanasse, J.; Wilkinson, K.J.; Sygusch, J.; Wilcox, D.E.; Omichinski, J.G.
    Structural 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 (2016), Biochemistry, 55, 1070-1081 .
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Priestia megaterium
expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant D99S, in complex with Cu(II), Hg and p-chloromercuribenzoate, to 1.24-1.95 A resolution Escherichia coli
to 1.24 A resolution, comparison with strucutre of Escherichia coli MerB mutant D99S Priestia megaterium

Protein Variants

Protein Variants Comment Organism
D99N Cu(II) is bound to the active site cysteine residues Escherichia coli
D99S mutation mimicks the sequence of Bacillus megaterium MerB. Cu(II) is bound to the active site cysteine residues and is displaced following the addition of either an organomercurial substrate or an ionic mercury product Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
copper paramagnetic Cu(II) is bound to the active site cysteine residues of mutant MerB D99S Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P77072
-
-
Priestia megaterium Q7DJN2 isoform MerB2
-

Purification (Commentary)

Purification (Comment) Organism
-
 Priestia megaterium
enzyme copurifies with bound Cu2+ Escherichia coli

Synonyms

Synonyms Comment Organism
merB
-
 Escherichia coli
MerB2
-
 Priestia megaterium