2hi7
From Proteopedia
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| - | [[Image:2hi7.gif|left|200px]] | + | [[Image:2hi7.gif|left|200px]] |
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| - | '''Crystal structure of DsbA-DsbB-ubiquinone complex''' | + | {{Structure |
| + | |PDB= 2hi7 |SIZE=350|CAPTION= <scene name='initialview01'>2hi7</scene>, resolution 3.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=UQ1:UBIQUINONE-1'>UQ1</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of DsbA-DsbB-ubiquinone complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HI7 is a [ | + | 2HI7 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HI7 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation., Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K, Ito K, Cell. 2006 Nov 17;127(4):789-801. PMID:[http:// | + | Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation., Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K, Ito K, Cell. 2006 Nov 17;127(4):789-801. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17110337 17110337] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: ubiquinone]] | [[Category: ubiquinone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:17:25 2008'' |
Revision as of 15:17, 20 March 2008
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| , resolution 3.70Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of DsbA-DsbB-ubiquinone complex
Overview
Oxidation of cysteine pairs to disulfide requires cellular factors present in the bacterial periplasmic space. DsbB is an E. coli membrane protein that oxidizes DsbA, a periplasmic dithiol oxidase. To gain insight into disulfide bond formation, we determined the crystal structure of the DsbB-DsbA complex at 3.7 A resolution. The structure of DsbB revealed four transmembrane helices and one short horizontal helix juxtaposed with Cys130 in the mobile periplasmic loop. Whereas DsbB in the resting state contains a Cys104-Cys130 disulfide, Cys104 in the binary complex is engaged in the intermolecular disulfide bond and captured by the hydrophobic groove of DsbA, resulting in separation from Cys130. This cysteine relocation prevents the backward resolution of the complex and allows Cys130 to approach and activate the disulfide-generating reaction center composed of Cys41, Cys44, Arg48, and ubiquinone. We propose that DsbB is converted by its specific substrate, DsbA, to a superoxidizing enzyme, capable of oxidizing this extremely oxidizing oxidase.
About this Structure
2HI7 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation., Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K, Ito K, Cell. 2006 Nov 17;127(4):789-801. PMID:17110337
Page seeded by OCA on Thu Mar 20 17:17:25 2008
Categories: Escherichia coli | Protein complex | Inaba, K. | Ito, K. | Murakami, S. | Nakagawa, A. | Okada, K. | Suzuki, M. | Yamashita, E. | UQ1 | ZN | Disulfide bond | Dsbb | Membrane protein | Oxidative protein folding | Redox | Ubiquinone
