2bjo

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==Overview==
==Overview==
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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.
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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.]]
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[[Category: Cooper, D.R.]]
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[[Category: Cooper, D R.]]
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[[Category: Derewenda, Z.S.]]
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[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:21:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:35 2008''

Revision as of 14:38, 21 February 2008


2bjo, resolution 2.101Å

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CRYSTAL STRUCTURE OF THE ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN OHRB OF BACILLUS SUBTILIS

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.

About this Structure

2BJO is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state., Cooper DR, Surendranath Y, Devedjiev Y, Bielnicki J, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1269-73. Epub 2007, Nov 16. PMID:18084074

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