| pubmed-article:7809062 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C0001465 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C0016755 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C0599739 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C1706498 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C1879746 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C1547011 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C2346521 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:7809062 | lifeskim:mentions | umls-concept:C0060767 | lld:lifeskim |
| pubmed-article:7809062 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:7809062 | pubmed:dateCreated | 1995-2-2 | lld:pubmed |
| pubmed-article:7809062 | pubmed:abstractText | The crystal structure of fructose-1,6-bisphosphatase (Fru-1,6-Pase; EC 3.1.3.11) complexed with Zn2+ and two allosteric regulators, AMP and fructose 2,6-bisphosphate (Fru-2,6-P2) has been determined at 2.0-A resolution. In the refined model, the crystallographic R factor is 0.189 with rms deviations of 0.014 A and 2.8 degrees from ideal geometries for bond lengths and bond angles, respectively. A 15 degrees rotation is observed between the upper dimer C1C2 and the lower dimer C3C4 relative to the R-form structure (fructose 6-phosphate complex), consistent with that expected from a T-form structure. The major difference between the structure of the previously determined Fru-2,6-P2 complex (R form) and that of the current quaternary T-form complex lies in the active site domain. A zinc binding site distinct from the three binding sites established earlier was identified within each monomer. Helix H4 (residues 123-127) was found to be better defined than in previously studied ligated Fru-1,6-Pase structures. Interactions between monomers in the active site domain were found involving H4 residues from one monomer and residues Tyr-258 and Arg-243 from the adjacent monomer. Cooperativity between AMP and Fru-2,6-P2 in signal transmission probably involves the following features: an AMP site, the adjacent B3 strand (residues 113-118), the metal site, the immediate active site, the short helix H4 (residues 123-127), and Tyr-258 and Arg-243 from the adjacent monomer within the upper (or lower) dimer. The closest distance between the immediate active site and that on the adjacent monomer is only 5 A. Thus, the involvement of H4 in signal transmission adds another important pathway to the scheme of the allosteric mechanism of Fru-1,6-Pase. | lld:pubmed |
| pubmed-article:7809062 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7809062 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7809062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7809062 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7809062 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:7809062 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:7809062 | pubmed:author | pubmed-author:LipscombW NWN | lld:pubmed |
| pubmed-article:7809062 | pubmed:author | pubmed-author:WuY VYV | lld:pubmed |
| pubmed-article:7809062 | pubmed:author | pubmed-author:HuangSS | lld:pubmed |
| pubmed-article:7809062 | pubmed:author | pubmed-author:ZhangYY | lld:pubmed |
| pubmed-article:7809062 | pubmed:author | pubmed-author:LiangJ YJY | lld:pubmed |
| pubmed-article:7809062 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7809062 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:7809062 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:7809062 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7809062 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7809062 | pubmed:pagination | 12482-6 | lld:pubmed |
| pubmed-article:7809062 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:meshHeading | pubmed-meshheading:7809062-... | lld:pubmed |
| pubmed-article:7809062 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7809062 | pubmed:articleTitle | Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 2,6-bisphosphate, AMP, and Zn2+ at 2.0-A resolution: aspects of synergism between inhibitors. | lld:pubmed |
| pubmed-article:7809062 | pubmed:affiliation | Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138. | lld:pubmed |
| pubmed-article:7809062 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7809062 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7809062 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:2203 | entrezgene:pubmed | pubmed-article:7809062 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7809062 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7809062 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7809062 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7809062 | lld:pubmed |
