Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
1995-2-2
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.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-1312721, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-14042694, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-17810339, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-1849642, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-1850623, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-2025413, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-2157849, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-2164670, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-3028056, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-6260770, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-6265919, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-6277165, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-6303063, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-6307691, http://linkedlifedata.com/resource/pubmed/commentcorrection/7809062-8382525
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12482-6
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1994
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.
pubmed:affiliation
Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.