The crystal structure of the protein YhaK from Escherichia coli reveals a new subclass of redox sensitive enterobacterial bicupins

↓ Direkt till sidans innehåll
↓ Direkt till sidans sekundära innehåll (sidomenyn)

Search: id:"swepub:oai:DiVA.org:su-17352" > The crystal structu...

1 of 1
Previous record
Next record
To hitlist

Details
MARC

Gurmu, DanielStockholms universitet,Institutionen för biokemi och biofysik (author)

The crystal structure of the protein YhaK from Escherichia coli reveals a new subclass of redox sensitive enterobacterial bicupins

Article/chapterEnglish2009

Publisher, publication year, extent ...

Wiley,2009
printrdacarrier

Numbers

LIBRIS-ID:oai:DiVA.org:su-17352
https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-17352URI
https://doi.org/10.1002/prot.22128DOI
http://kipublications.ki.se/Default.aspx?queryparsed=id:118019020URI

Supplementary language notes

Language:English
Summary in:English

Part of subdatabase

SwePubSwePub

Classification

Subject category:ref swepub-contenttype
Subject category:art swepub-publicationtype

Notes

YhaK is a protein of unknown function found in low abundance in the cytosol of Escherichia coli. DNA array studies have revealed that YhaK is strongly up-regulated by nitroso-glutathione (GSNO) and also displays a 12-fold increase in expression during biofilm growth of E. coli 83972 and VR50 in human urine. We have determined the YhaK crystal structure and demonstrated that in vitro YhaK is a good marker for monitoring oxidative stresses in E. coli. The YhaK protein structure shows a bicupin fold where the two cupin domains are crosslinked with one intramolecular disulfide bond (Cys10 to Cys204). We found that the third cysteine in YhaK, Cys122, is oxidized to a sulfenic acid. Two chloride ions are found in the structure, one close to the reactive Cys122, and the other on a hydrophobic surface close to a symmetry-related molecule. There are major structural differences at the N-terminus of YhaK compared with similar structures that also display the bicupin fold (YhhW and hPirin). YhaK showed no quercetinase and peroxidase activity. However, reduced YhaK was very sensitive to reactive oxygen species (ROS). The complete, functional E. coli glutaredoxin or thioredoxin systems protected YhaK from oxidation. E. coli thioredoxin reductase and NADPH produced ROS and caused oxidation and oligomerization of reduced YhaK. Taken together, we propose that YhaK is the first of a new sub-class of bicupins that lack the canonical cupin metal-binding residues of pirins and may be involved in chloride binding and/or sensing of oxidative stress in enterobacteria.

Added entries (persons, corporate bodies, meetings, titles ...)

Lu, JunKarolinska Institutet (author)
Johnson, Kenneth A. (author)
Nordlund, PärKarolinska Institutet (author)
Holmgren, Arne (author)
Erlandsen, Heidi (author)
Stockholms universitetInstitutionen för biokemi och biofysik (creator_code:org_t)

Related titles

In:Proteins: Wiley74:1, s. 18-310887-35851097-0134

Internet link

Find in a library

Proteins (Search for host publication in LIBRIS)

To the university's database

1 of 1
Previous record
Next record
To hitlist

Find more in SwePub

By the author/editor: Gurmu, Daniel; Lu, Jun; Johnson, Kenneth ...; Nordlund, Pär; Holmgren, Arne; Erlandsen, Heidi

Articles in the publication: Proteins

By the university: Stockholm University; Karolinska Institutet

Search outside SwePub

Extend your search to:: Google; Google Book Search; Google Scholar

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

LIBRIS.kb.se