| pubmed-article:11123916 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11123916 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:11123916 | lifeskim:mentions | umls-concept:C0401925 | lld:lifeskim |
| pubmed-article:11123916 | lifeskim:mentions | umls-concept:C0014230 | lld:lifeskim |
| pubmed-article:11123916 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:11123916 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:11123916 | lifeskim:mentions | umls-concept:C2346927 | lld:lifeskim |
| pubmed-article:11123916 | pubmed:issue | 51 | lld:pubmed |
| pubmed-article:11123916 | pubmed:dateCreated | 2001-1-8 | lld:pubmed |
| pubmed-article:11123916 | pubmed:abstractText | The monomeric homing endonuclease PI-SceI harbors two catalytic centers which cooperate in the cleavage of the two strands of its extended recognition sequence. Structural and biochemical data suggest that catalytic center I contains Asp218, Asp229, and Lys403, while catalytic center II contains Asp326, Thr341, and Lys301. The analogy with I-CreI, for which the cocrystal structure with the DNA substrate has been determined, suggests that Asp218 and Asp229 in catalytic center I and Asp326 and Thr341 in catalytic center II serve as ligands for Mg(2+), the essential divalent metal ion cofactor which can be replaced by Mn(2+) in vitro. We have carried out a mutational analysis of these presumptive Mg(2+) ligands. The variants carrying an alanine or asparagine substitution bind DNA, but (with the exception of the D229N variant) are inactive in DNA cleavage in the presence of Mg(2+), demonstrating that these residues are important for cleavage. Our finding that the PI-SceI variants carrying single cysteine substitutions at these positions are inactive in the presence of the oxophilic Mg(2+) but active in the presence of the thiophilic Mn(2+) suggests that the amino acid residues at these positions are involved in cofactor binding. From the fact that in the presence of Mn(2+) the D218C and D326C variants are even more active than the wild-type enzyme, it is concluded that Asp218 and Asp326 are the principal Mg(2+) ligands of PI-SceI. On the basis of these findings and the available structural information, a model for the composition of the two Mg(2+) binding sites of PI-SceI is proposed. | lld:pubmed |
| pubmed-article:11123916 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11123916 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11123916 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11123916 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11123916 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11123916 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:11123916 | pubmed:author | pubmed-author:PingoudAA | lld:pubmed |
| pubmed-article:11123916 | pubmed:author | pubmed-author:WendtFF | lld:pubmed |
| pubmed-article:11123916 | pubmed:author | pubmed-author:PingoudVV | lld:pubmed |
| pubmed-article:11123916 | pubmed:author | pubmed-author:SchöttlerSS | lld:pubmed |
| pubmed-article:11123916 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11123916 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:11123916 | pubmed:volume | 39 | lld:pubmed |
| pubmed-article:11123916 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11123916 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11123916 | pubmed:pagination | 15895-900 | lld:pubmed |
| pubmed-article:11123916 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11123916 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11123916 | pubmed:articleTitle | Identification of Asp218 and Asp326 as the principal Mg2+ binding ligands of the homing endonuclease PI-SceI. | lld:pubmed |
| pubmed-article:11123916 | pubmed:affiliation | Institut für Biochemie, FB 08, Justus-Liebig-Universität, Heinrich-Buff-Ring 58, D-35392 Giessen, Germany. | lld:pubmed |
| pubmed-article:11123916 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11123916 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:11123916 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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