Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE)

Disulfide‐bond (Dsb) proteins are a family of redox proteins containing a Cys‐X‐X‐Cys motif. They are essential for disulfide‐bond exchange in the bacterial periplasm and are necessary for the correct folding and function of many secreted proteins. CcmG (DsbE) is a reducing Dsb protein required for...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-09, Vol.57 (9), p.1293-1295
Main Authors: Edeling, Melissa A., Guddat, Luke W., Fabianek, Renata A., Halliday, Judy A., Jones, Alun, Thöny-Meyer, Linda, Martin, Jennifer L.
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Bradyrhizobium - chemistry
Crystallization
Crystallography, X-Ray
cytochrome c maturation
disulfide oxidoreductase
Dsb proteins
Oxidoreductases - biosynthesis
Oxidoreductases - chemistry
Oxidoreductases - genetics
Periplasmic Proteins
Protein Conformation
Selenomethionine - chemistry
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Summary:Disulfide‐bond (Dsb) proteins are a family of redox proteins containing a Cys‐X‐X‐Cys motif. They are essential for disulfide‐bond exchange in the bacterial periplasm and are necessary for the correct folding and function of many secreted proteins. CcmG (DsbE) is a reducing Dsb protein required for cytochrome c maturation. Crystals of Bradyrhizobium japonicum CcmG have been obtained that diffract X‐rays to 1.14 Å resolution. The crystals are orthorhombic, space group P212121, with unit‐cell parameters a = 35.1, b = 48.2, c = 90.2 Å. Selenomethionine CcmG was expressed without using a methionine auxotroph or methionine‐pathway inhibition and was purified without reducing agents.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444901009982