Literature summary for 1.8.4.12 extracted from

Kauffmann, B.; Favier, F.; Olry, A.; Boschi-Muller, S.; Carpentier, P.; Branlant, G.; Aubry, A.
Crystallization and preliminary X-ray diffraction studies of the peptide methionine sulfoxide reductase B domain of Neisseria meningitidis PILB (2002), Acta Crystallogr. Sect. D, 58, 1467-1469.

Search for more literature for 1.8.4.12

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of the MsrB domain in Escherichia coli, strain B834(DE3) produces a selenomethionine-substituted MsrB	Neisseria meningitidis

Crystallization (Commentary)

Crystallization (Comment)	Organism
selenomethionine-substituted peptide methionine sulfoxide reductase B domain, hanging drop vapour diffusion method in multiwell tissue-culture plates, 0.004 ml protein solution containing 75 mg/ml protein in 50 mM Tris-HCl, pH 8.0, mixed with 0.004 ml precipitant solution at 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.8 A resolution	Neisseria meningitidis

Organism

Organism	UniProt	Comment	Textmining
Neisseria meningitidis	-	enzyme PILB, a peptide methionine sulfoxide reductase with 2 subdomains MsrA and MsrB with opposite stereospecificity, MsrA activity belongs to EC 1.8.4.B2	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant MsrB domain from Escherichia coli	Neisseria meningitidis

Subunits

Subunits	Comment	Organism
?	x * 16372.0, recombinant MsrB, mass spectrometry, x * 16467.2, recombinant selenomethionine-MsrB, mass spectrometry	Neisseria meningitidis

Synonyms

Synonyms	Comment	Organism
MSR	-	Neisseria meningitidis
peptide methionine sulfoxide reductase	-	Neisseria meningitidis
PilB	-	Neisseria meningitidis

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Release 2023.1 (January 2023)