Structure of a bacterial homologue of vitamin K epoxide reductase (Q27659264)

2

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author name string

Weikai Li

1

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Rachel J Dutton

3

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Dana Boyd

4

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Jon Beckwith

Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB

5

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language of work or name

English

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publication date

28 January 2010

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published in

Nature

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volume

463

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issue

7280

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page(s)

507-12

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cites work

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Vitamin K epoxide reductase: homology, active site and catalytic mechanism

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Mutations in VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2

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Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation.

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Structure and function of vitamin K epoxide reductase

29 September 2017

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The conversion of vitamin K epoxide to vitamin K quinone and vitamin K quinone to vitamin K hydroquinone uses the same active site cysteines

29 September 2017

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Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2

29 September 2017

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Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction

29 September 2017

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Disulfide bond formation involves a quinhydrone-type charge–transfer complex

29 September 2017

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Vitamin K-Dependent Formation of γ-Carboxyglutamic Acid

29 September 2017

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Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomerase

29 September 2017

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2 June 2018

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Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation.

27 November 2018

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Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation.

27 November 2018

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DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.

27 November 2018

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Phase combination and cross validation in iterated density-modification calculations

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12 December 2020

A new vitamin K epoxide reductase complex subunit-1 (VKORC1) mutation in a patient with decreased stability of CYP2C9 enzyme

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12 December 2020

[4] Combining constraints for electron-density modification

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12 December 2020

Processing of X-ray diffraction data collected in oscillation mode

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12 December 2020

DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA

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Reconstitution of a protein disulfide catalytic system

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12 December 2020