Linked Life Data

18759453

Source:http://linkedlifedata.com/resource/pubmed/id/18759453

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
38
pubmed:dateCreated
2008-9-16
pubmed:databankReference
pubmed:abstractText
Escherichia coli and related bacteria require nickel for the synthesis of hydrogenases, enzymes involved in hydrogen oxidation and proton reduction. Nickel transport to the cytoplasm depends on five proteins, NikA-E. We have previously reported the three-dimensional structure of the soluble periplasmic nickel transporter NikA in a complex with FeEDTA(H 2O) (-). We have now determined the structure of EDTA-free NikA and have found that it binds a small organic molecule that contributes three ligands to the coordination of a transition metal ion. Unexpectedly, His416, which was far from the metal-binding site in the FeEDTA(H 2O) (-)-NikA complex, becomes the fourth observed ligand to the metal. The best match to the omit map electron density is obtained for butane-1,2,4-tricarboxylate (BTC). Our attempts to obtain a BTC-Ni-NikA complex using apo protein and commercial reagents resulted in nickel-free BTC-NikA. Overall, our results suggest that nickel transport in vivo requires a specific metallophore that may be BTC.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
23
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9937-43
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Structural characterization of a putative endogenous metal chelator in the periplasmic nickel transporter NikA.
pubmed:affiliation
Laboratoire de Cristallographie et de Cristallogenese des Proteines, Institut de Biologie Structurale J.P. Ebel, CEA, CNRS, Universite J. Fourier, 41 rue J. Horowitz, 38027 Grenoble Cedex 1, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't