| pubmed-article:16989860 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16989860 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:16989860 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16989860 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:16989860 | lifeskim:mentions | umls-concept:C0376522 | lld:lifeskim |
| pubmed-article:16989860 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16989860 | lifeskim:mentions | umls-concept:C1707719 | lld:lifeskim |
| pubmed-article:16989860 | lifeskim:mentions | umls-concept:C0661851 | lld:lifeskim |
| pubmed-article:16989860 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16989860 | pubmed:dateCreated | 2006-10-18 | lld:pubmed |
| pubmed-article:16989860 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16989860 | pubmed:abstractText | Acireductone dioxygenase (ARD) catalyzes different reactions between O2 and 1,2-dihydroxy-3-oxo-5-(methylthio)pent-1-ene (acireductone) depending upon the metal bound in the active site. Ni2+ -ARD cleaves acireductone to formate, CO and methylthiopropionate. If Fe2+ is bound (ARD'), the same substrates yield methylthioketobutyrate and formate. The two forms differ in structure, and are chromatographically separable. Paramagnetism of Fe2+ renders the active site of ARD' inaccessible to standard NMR methods. The structure of ARD' has been determined using Fe2+ binding parameters determined by X-ray absorption spectroscopy and NMR restraints from H98S ARD, a metal-free diamagnetic protein that is isostructural with ARD'. ARD' retains the beta-sandwich fold of ARD, but a structural entropy switch increases order at one end of a two-helix system that bisects the beta-sandwich and decreases order at the other upon interconversion of ARD and ARD', causing loss of the C-terminal helix in ARD' and rearrangements of residues involved in substrate orientation in the active site. | lld:pubmed |
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| pubmed-article:16989860 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16989860 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16989860 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16989860 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16989860 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16989860 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:16989860 | pubmed:author | pubmed-author:PochapskySusa... | lld:pubmed |
| pubmed-article:16989860 | pubmed:author | pubmed-author:PochapskyThom... | lld:pubmed |
| pubmed-article:16989860 | pubmed:author | pubmed-author:JuTingtingT | lld:pubmed |
| pubmed-article:16989860 | pubmed:author | pubmed-author:MaroneyMichae... | lld:pubmed |
| pubmed-article:16989860 | pubmed:author | pubmed-author:ChaiSergio... | lld:pubmed |
| pubmed-article:16989860 | pubmed:author | pubmed-author:GoldsmithRach... | lld:pubmed |
| pubmed-article:16989860 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16989860 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:16989860 | pubmed:volume | 363 | lld:pubmed |
| pubmed-article:16989860 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16989860 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16989860 | pubmed:pagination | 823-34 | lld:pubmed |
| pubmed-article:16989860 | pubmed:dateRevised | 2011-3-22 | lld:pubmed |
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| pubmed-article:16989860 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16989860 | pubmed:articleTitle | One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase. | lld:pubmed |
| pubmed-article:16989860 | pubmed:affiliation | Department of Chemistry, Brandeis University, MS 015, Waltham, MA 02454-9110, USA. | lld:pubmed |
| pubmed-article:16989860 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16989860 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16989860 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16989860 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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