Purification and properties of the Klebsiella aerogenes UreE metal-binding domain, a functional metallochaperone of urease.
Klebsiella aerogenes UreE, a metallochaperone that delivers nickel ions during urease activation, consists of distinct "peptide-binding" and "metal-binding" domains and a His-rich C terminus. Deletion analyses revealed that the metal-binding domain alone is sufficient to facilitate urease activation. This domain was purified and shown to exhibit metal-binding properties similar to those of UreE lacking only the His-rich tail.
Mulrooney
Scott B
SB
Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan 48824-4320, USA.
Ward
Sarah K
SK
Hausinger
Robert P
RP
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D021902:Enterobacter aerogenes / Q000235:genetics / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism; D010957:Plasmids; D017434:Protein Structure, Tertiary; D014510:Urease / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D008670:Metals; D018832:Molecular Chaperones; C090404:UreE protein, Bacteria; D014510:Urease