| pubmed-article:12514740 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12514740 | lifeskim:mentions | umls-concept:C0016223 | lld:lifeskim |
| pubmed-article:12514740 | lifeskim:mentions | umls-concept:C0033385 | lld:lifeskim |
| pubmed-article:12514740 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:12514740 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:12514740 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12514740 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:12514740 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:12514740 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12514740 | pubmed:dateCreated | 2003-1-29 | lld:pubmed |
| pubmed-article:12514740 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12514740 | pubmed:abstractText | The PutA flavoprotein from Escherichia coli plays multiple roles in proline catabolism by functioning as a membrane-associated bi-functional enzyme and a transcriptional repressor of proline utilization genes. The human homolog of the PutA proline dehydrogenase (PRODH) domain is critical in p53-mediated apoptosis and schizophrenia. Here we report the crystal structure of a 669-residue truncated form of PutA that shows both PRODH and DNA-binding activities, representing the first structure of a PutA protein and a PRODH enzyme from any organism. The structure is a domain-swapped dimer with each subunit comprising three domains: a helical dimerization arm, a 120-residue domain containing a three-helix bundle similar to that in the helix-turn-helix superfamily of DNA-binding proteins and a beta/alpha-barrel PRODH domain with a bound lactate inhibitor. Analysis of the structure provides insight into the mechanism of proline oxidation to pyrroline-5-carboxylate, and functional studies of a mutant protein suggest that the DNA-binding domain is located within the N-terminal 261 residues of E. coli PutA. | lld:pubmed |
| pubmed-article:12514740 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12514740 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12514740 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12514740 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12514740 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12514740 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12514740 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12514740 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12514740 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12514740 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12514740 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12514740 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:12514740 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:12514740 | pubmed:author | pubmed-author:AroAA | lld:pubmed |
| pubmed-article:12514740 | pubmed:author | pubmed-author:LeeYong-HwanY... | lld:pubmed |
| pubmed-article:12514740 | pubmed:author | pubmed-author:BeckerDonald... | lld:pubmed |
| pubmed-article:12514740 | pubmed:author | pubmed-author:TannerJohn... | lld:pubmed |
| pubmed-article:12514740 | pubmed:author | pubmed-author:NadaraiaShore... | lld:pubmed |
| pubmed-article:12514740 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12514740 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:12514740 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12514740 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12514740 | pubmed:pagination | 109-14 | lld:pubmed |
| pubmed-article:12514740 | pubmed:dateRevised | 2011-3-15 | lld:pubmed |
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| pubmed-article:12514740 | pubmed:meshHeading | pubmed-meshheading:12514740... | lld:pubmed |
| pubmed-article:12514740 | pubmed:meshHeading | pubmed-meshheading:12514740... | lld:pubmed |
| pubmed-article:12514740 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12514740 | pubmed:articleTitle | Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein. | lld:pubmed |
| pubmed-article:12514740 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Missouri-Columbia, 65211, USA. | lld:pubmed |
| pubmed-article:12514740 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12514740 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12514740 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| literatureCitation:3254_125... | literatureCitation:pubmed | pubmed-article:12514740 | lld:drugbank |
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