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1frp
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(New page: 200px<br /><applet load="1frp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frp, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 13:05, 20 November 2007
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CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE-2,6-BISPHOSPHATE, AMP AND ZN2+ AT 2.0 ANGSTROMS RESOLUTION. ASPECTS OF SYNERGISM BETWEEN INHIBITORS
Overview
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.
About this Structure
1FRP is a Single protein structure of sequence from Sus scrofa with FDP, ZN and AMP as ligands. Active as Fructose-bisphosphatase, with EC number 3.1.3.11 Full crystallographic information is available from OCA.
Reference
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., Xue Y, Huang S, Liang JY, Zhang Y, Lipscomb WN, Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12482-6. PMID:7809062
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