Linked Life Data

11955067

Source:http://linkedlifedata.com/resource/pubmed/id/11955067

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2002-4-16
pubmed:databankReference
pubmed:abstractText
Taurine/alpha-ketoglutarate dioxygenase (TauD), a non-heme Fe(II) oxygenase, catalyses the conversion of taurine (2-aminoethanesulfonate) to sulfite and aminoacetaldehyde concurrent with the conversion of alpha-ketoglutarate (alphaKG) to succinate and CO(2). The enzyme allows Escherichia coli to use taurine, widely available in the environment, as an alternative sulfur source. Here we describe the X-ray crystal structure of TauD complexed to Fe(II) and both substrates, alphaKG and taurine. The tertiary structure and fold of TauD are similar to those observed in other enzymes from the broad family of Fe(II)/alphaKG-dependent oxygenases, with closest structural similarity to clavaminate synthase. Using the TauD coordinates, a model was determined for the closely related enzyme 2,4-dichlorophenoxyacetate/alphaKG dioxygenase (TfdA), supporting predictions derived from site-directed mutagenesis and other studies of that biodegradative protein. The TauD structure and TfdA model define the metal ligands and the positions of nearby aromatic residues that undergo post-translational modifications involving self-hydroxylation reactions. The substrate binding residues of TauD were identified and those of TfdA predicted. These results, along with sequence alignment information, reveal how TauD selects a tetrahedral substrate anion in preference to the planar carboxylate selected by TfdA, providing insight into the mechanism of enzyme catalysis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5185-92
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11955067-2,4-Dichlorophenoxyacetic Acid, pubmed-meshheading:11955067-Amino Acid Sequence, pubmed-meshheading:11955067-Binding Sites, pubmed-meshheading:11955067-Catalysis, pubmed-meshheading:11955067-Crystallization, pubmed-meshheading:11955067-Crystallography, X-Ray, pubmed-meshheading:11955067-Dimerization, pubmed-meshheading:11955067-Escherichia coli, pubmed-meshheading:11955067-Ferrous Compounds, pubmed-meshheading:11955067-Ketoglutaric Acids, pubmed-meshheading:11955067-Mixed Function Oxygenases, pubmed-meshheading:11955067-Models, Molecular, pubmed-meshheading:11955067-Molecular Sequence Data, pubmed-meshheading:11955067-Protein Processing, Post-Translational, pubmed-meshheading:11955067-Protein Structure, Secondary, pubmed-meshheading:11955067-Substrate Specificity, pubmed-meshheading:11955067-Taurine
pubmed:year
2002
pubmed:articleTitle
X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates.
pubmed:affiliation
Dyson Perrins Laboratory, Oxford University, South Parks Road, Oxford, England, OX1 3QY, and Departments of Microbiology & Molecular Genetics and Biochemistry & Molecular Biology, Michigan State University, East Lansing, Michigan 48824-1011.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't