{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,7]],"date-time":"2026-01-07T22:18:58Z","timestamp":1767824338271,"version":"3.49.0"},"reference-count":45,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2008,6,16]],"date-time":"2008-06-16T00:00:00Z","timestamp":1213574400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2009,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>YhaK is a protein of unknown function found in low abundance in the cytosol of <jats:italic>Escherichia coli<\/jats:italic>. DNA array studies have revealed that YhaK is strongly up\u2010regulated by nitroso\u2010glutathione (GSNO) and also displays a 12\u2010fold increase in expression during biofilm growth of <jats:italic>E. coli<\/jats:italic> 83972 and VR50 in human urine. We have determined the YhaK crystal structure and demonstrated that <jats:italic>in vitro<\/jats:italic> YhaK is a good marker for monitoring oxidative stresses in <jats:italic>E. coli<\/jats:italic>. 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\u2010related molecule. There are major structural differences at the N\u2010terminus 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 <jats:italic>E. coli<\/jats:italic> glutaredoxin or thioredoxin systems protected YhaK from oxidation. <jats:italic>E. coli<\/jats:italic> 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\u2010class of bicupins that lack the canonical cupin metal\u2010binding residues of pirins and may be involved in chloride binding and\/or sensing of oxidative stress in enterobacteria. Proteins 2009. \u00a9 2008 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.22128","type":"journal-article","created":{"date-parts":[[2008,6,16]],"date-time":"2008-06-16T18:02:21Z","timestamp":1213639341000},"page":"18-31","source":"Crossref","is-referenced-by-count":23,"title":["The crystal structure of the protein YhaK from <i>Escherichia coli<\/i> reveals a new subclass of redox sensitive enterobacterial bicupins"],"prefix":"10.1002","volume":"74","author":[{"given":"Daniel","family":"Gurmu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jun","family":"Lu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kenneth 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