2bjo: Difference between revisions

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==Overview==
==Overview==
The crystal structure of the fully oxidized form of the Bacillus subtilis, organic hydroperoxide-resistance (OhrB) protein is reported at 2.1 A, resolution. The electron density reveals an intact catalytic disulfide, bond (Cys55-Cys119) in each of the two molecules, which are intertwined, into a canonical obligate dimer. However, the stereochemistry of the, disulfides is unorthodox and strained, suggesting that they are sensitive, to reducing agents. A deep solvent-accessible gorge reaching Cys55 may, represent the access route for the reductant.
The crystal structure of the fully oxidized form of the Bacillus subtilis organic hydroperoxide-resistance (OhrB) protein is reported at 2.1 A resolution. The electron density reveals an intact catalytic disulfide bond (Cys55-Cys119) in each of the two molecules, which are intertwined into a canonical obligate dimer. However, the stereochemistry of the disulfides is unorthodox and strained, suggesting that they are sensitive to reducing agents. A deep solvent-accessible gorge reaching Cys55 may represent the access route for the reductant.


==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bielnicki, J.]]
[[Category: Bielnicki, J.]]
[[Category: Cooper, D.R.]]
[[Category: Cooper, D R.]]
[[Category: Derewenda, Z.S.]]
[[Category: Derewenda, Z S.]]
[[Category: Devedjiev, Y.]]
[[Category: Devedjiev, Y.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


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